BINDING DOMAINS FROM PLASMODIUM VIVAX AND PLASMODIUM FALCIPARUM ERYTHROCYTE BINDING PROTEINS

Abstract: The present invention provides isolated polypeptides useful in the treatment and prevention of malaria caused by Plasmodium falciparum or P. vivax. In particular, the polypeptides are derived from the binding domains of the proteins in the EBL family as well as the sialic acid binding protein (SABP) on P. falciparum merozoites. The polypeptides may also be derived from the Duffy antigen binding protein (DABP) on P. vivax merozoites.

Description: BINDINGDOMAINSFROMPLASMODIUMVIVAX ANDPLASMODIUMFALCIPARUMERYTHROCYTE BINDINGPROTEINS BACKGROUND OF THE INVENTION Malaria infects 200 - 400 million people each year causing 1-2 million deaths, thus remaining one of the most important infectious diseases in the world. Approximately 25 percent of all deaths of children in rural Africa between the ages of one and four years are caused by malaria. Due to the importance of the disease as a worldwide health problem, considerable effort is being expended to identify and develop malaria vaccines. Malaria in humans is caused by four species of the parasite Plasmodiu : P. falciparum, P. vivax, P . knowlesi and P. malariae . The major cause of malaria in humans if P. falciparum which infects 200 million to 400 million people every year, killing 1 to 4 million. P. vivax (one of the four species infective to humans) cannot be cultured in vitro, as has been possible with P. knowlesi (a malarial strain found in old world monkeys which also invade human erythrocytes) and P. falciparum. Although P. vivax bears substantial phylogenetic similarity to P. knowlesi , the two species are different in many important respects. For example, P. vivax is not infective of many simian species and infection is poorly established in others, whereas P. knowlesi is poorly infective of humans while readily infecting many simian species. The basis of various potential vaccines to combat malaria is appreciated through an understanding of the life cycle of the parasite. Infection in humans begins when young malarial parasites or "sporozoites" are injected into the bloodstream of a human by the mosquito. Following injection, the parasite localizes to liver cells. After approximately one week the parasites or "merozoites" are released into the bloodstream. The entry of the parasites into the bloodstream begins the "erythrocytic" phase. Each parasite enters the red blood cell in order to grow and develop. When the merozoite matures in the red blood cell, it is known as a trophozoite. The trophozoite undergoes several rounds of nuclear division (schizogony) until it ruptures the erythrocyte, releasing from 6 to 24 merozoites. After several asexual schizogonic cycles, some parasites, instead of becoming schizonts through asexual reproduction, develop into morphologically distinct forms known as "gametocytes" which are long-lived and undergo sexual development. Sexual development of the malaria parasites involve the female or "macrogametocyte" and the male parasite or "microgametocyte." These gametocytes do not undergo any further development in humans. Upon ingestion of the gametocytes into the mosquito, the complicated sexual cycle begins in the midgut of the mosquito. The red blood cells disintegrate in the midgut of the mosquito after 1 0 to 20 minutes. The microgametocyte continues to develop through exflagellation and releases 8 highly flagellated microgametes. Fertilization occurs upon fusion of the icrogamete and the macrogamete. The fertilized parasite is known as a zygote which develops into an "ookinete." The ookinete embeds in the midgut of the mosquito, transforming into an oocyst within which many small sporozoites form. Before embedding in the midgut, the ookinete must first penetrate the peritrophic membrane which apparently acts as a barrier for invasion of ingested parasites. When the oocyst ruptures the sporozoites migrate to the salivary gland of the mosquito via the hemolymph. Once in the saliva of the mosquito, the parasite can be injected into a host. The erythrocytic stage of the Plasmodium life cycle is of special relevance to vaccine development because the clinical and pathologic features of malaria in the host are attributable to this stage. In P. vivax, and P. knowlesi , Duffy blood group determinants present on Duffy positive erythrocytes are essential for invasion of human erythrocytes (Miller et al . , Science 189: 561-563, (1975); Miller et al., N. Engl. J. Med. 295: 302-304, (1976)). In P. falciparum, invasion of merozoites into erythrocytes appears to be dependent on binding to sialic acids on glycophorins on the erythrocyte (Miller, et al . , J. Exp. Med. 146: 277-281, (1971); Pasvol, et al . , Lancet, ii: 947-950 (1982); Pasvol, et al . , Nature, 279: 64-66 (1982); Perkins, J. Exp. Med. 160: 788-798 (1984)). Studies with the monkey parasite P. knowlesi allow a clearer understanding of the multiple events that occur during invasion. It is likely that even though P. vivax and P. falciparum bind to the Duffy antigen and sialic acids respectively, they share common strategies of invasion with each other and with P. knowlesi . In P. knowlesi , during invasion a merozoite first attaches to an erythrocyte on any surface of the merozoite, then reorients so that its apical end is in contact with the erythrocyte (Dvorak et al . , Science 187: 748-750, (1975)). Both attachment and reorientation of merozoites occur equally well on Duffy positive and Duffy negative cells. A junction then forms between the apical end of the merozoite and the Duffy positive erythrocyte followed by vacuole formation and entry of the merozoite into the vacuole. Aikawa et al . , J. Cell Biol. 77: 72-82 (1978) . Junction formation and merozoite entry into the erythrocyte do not occur on Duffy negative cells (Miller et al . , J. Exp. Med. 149: 172-184 (1979)), suggesting that a receptor specific for the Duffy determinant is involved in apical junction formation but not initial attachment. The apical end of the merozoite is defined by the presence of three organelles: rhopteries, dense granules and micronemes. The rhopteries and dense granules release their contents at vacuole formation (Ladda et al . , 1969; Aikawa et al . , J. Cell Biol., 77: 72-82 (1978); Torn et al. , Infection and Immunity 57: 3230-3233 (1989) ; Bannister and Dluzewski, Blood Cells 16: 257-292 (1990)). To date the function of the microneme is unknown. Nevertheless, the location of the micronemes suggest that they are involved in the invasion process. Duffy Antigen Binding Protein (DABP) and Sialic Acid Binding Protein (SABP) have been localized to the micronemes of P. knowlesi and P . falciparum respectively (Adams et al . t Cell 63: 141-153 (1990); Sim et al . , Mol. Biochem. Parasitol. 51: 157-160 (1992) ) . DABP and SABP are soluble proteins that appear in the culture supernatant after infected erythrocytes release merozoites. Immunochemical data indicate that DABP and SABP which are the respective ligands for the P. vivax and P. falciparum Duffy and sialic acid receptors on erythrocytes, possess specificities of binding which are identical either in soluble or membrane bound form. DABP is a 135 kDa protein which binds specifically to Duffy blood group determinants ( ertheimer et ai., Exp. Parasitol. 69: 340-350 (1989); Barnwell, et al . , J. Exp. Med. 169: 1795-1802 (1989)). Thus, binding of DABP is specific to human Duffy positive erythrocytes. There are four major Duffy phenotypes for human erythrocytes: Fy(a) , Fy(b) , Fy(ab) and Fy(negative) , as defined by the anti-Fy a and anti-Fy* 5 sera (Hadley et al . , In Red Cell Antigens and Antibodies, G. Garratty, ed. (Arlington, Va.:American Association of Blood Banks) pp. 17-33 (1986)). DABP binds equally to both Fy(a) and Fy(b) erythrocytes which are equally susceptible to invasion by P. vivax; but not to Fy(negative) erythrocytes. In the case of SABP, a 175kDa protein, binding is specific to the glycophorin sialic acid residues on erythrocytes (Camus and Hadley, Science 230:553-556 (1985); Orlandi, et al . , J. Cell Biol. 116:901-909 (1992)). Thus, neuraminidase treatment (which cleaves off sialic acid residues) render erythrocytes immune to P. falciparum invasion. The specificities of binding and correlation to invasion by the parasite thus indicate that DABP and SABP are the proteins of P. vivax and P. falciparum which interact with sialic acids and the Duffy antigen on the erythrocyte. The genes encoding both proteins have been cloned and the DNA and predicted protein sequences have been determined (B. Kim Lee Sim, et al . , J. Cell Biol. Ill: 1877-1884 (1990); Fang, X., et al . , Mol. Biochem Parasitol. 44: 125-132 (1991)). Despite considerable research efforts worldwide, because of the complexity of the Plasmodium parasite and its interaction with its host, it has not been possible to discover a satisfactory solution for prevention or abatement of the blood stage of malaria. Because malaria is a such a large worldwide health problem, there is a need for methods that abate the impact of this disease. The present invention provides effective preventive and therapeutic measures against Plasmodium invasion. SUMMARY OF THE INVENTION The present invention provides compositions comprising an isolated DABP binding domain polypeptides and/or isolated SABP binding domain polypeptides. The DABP binding domain polypeptides preferably comprise between about 200 and about 300 amino acid residues while the SABP binding domain polypeptides preferably comprises between about 200 and about 600 amino acid residues. A preferred DABP binding domain polypeptide has residues 1 to about 325 of the amino acid sequence found in SEQ ID No. 2. A preferred SABP binding domain polypeptide has residues l to about 616 of the amino acid sequence of SEQ ID No. 4. The present invention also includes pharmaceutical compositions comprising a pharmaceutically acceptable carrier and an isolated DABP binding domain polypeptide in an amount sufficient to induce a protective immune response, to Plasmodium vivax merozoites in an organism. In addition, isolated SABP binding domain polypeptide in an amount sufficient to induce a protective immune response to Plasmodium falciparum may be added to the pharmaceutical composition. Also provided are pharmaceutical compositions comprising a pharmaceutically acceptable carrier and an isolated SABP binding domain polypeptide in an amount sufficient to induce a protective immune response to Plasmodium falciparum merozoites in an organism. In addition, isolated DABP binding domain polypeptide in an amount sufficient to induce a protective immune response to Plasmodium vivax may be added to the pharmaceutical composition. Isolated polynucleotides which encode a DABP binding domain polypeptides or SABP binding domain polypeptides are also disclosed. In addition, the present invention includes a recombinant cell comprising the polynucleotide encoding the DABP binding domain polypeptide. The current invention further includes methods of inducing a protective immune response to Plasmodium merozoites in a patient. The methods comprise administering to the patient an immunologically effective amount of a pharmaceutical composition comprising a pharmaceutically acceptable carrier and an isolated DABP binding domain polypeptide, an SABP binding domain polypeptide or a combination thereof. The present disclosure also provides DNA sequences from additional P. falciparum genes in the erythrocyte binding ligand (.EBL) family that have regions conserved with the P. falciparum 175 kD and P. vivax 135 kD binding proteins. DEFINITIONS As used herein a "DABP binding domain polypeptide" or a "SABP binding domain polypeptide" are polypeptides substantially identical (as defined below) to a sequence from the cysteine-rich, amino-terminal region of the Duffy antigen binding protein (DABP) or sialic acid binding protein (SABP) , respectively. Such polypeptides are capable of binding either the Duffy antigen or sialic acid residues on glycophorin. In particular, DABP binding domain polypeptides consist of amino acid residues substantially similar to a sequence of SABP within a binding domain from the N-terminal amino acid (residue 1) to about residue 325. SABP binding domain polypeptides consist of residues substantially similar to a sequence of DABP within a binding domain from the N-terminal amino acid (residue 1) to about residue 616. The binding domain polypeptides encoded by the genes of the EBL family consist of those residues substantially identical to the sequence of the binding domains of DABP and SABP as defined above. The EBL family comprises sequences with substantial similarity to the conserved regions of the DABP and SABP. These include those sequences reported here as EBL-el (SEQ ID NOs 5 and 6) , E31a (SEQ ID NOs 7 and 8), EBL- e2 (SEQ ID NOs 9 and 10) and Proj3 (SEQ ID NOs 11 and 12). The polypeptides of the invention can consist of the full length binding domain or a fragment thereof. Typically DABP binding domain polypeptides will consist of from about 50 to about 325 residues, preferably between about 75 and 300, more preferably between about 100 and about 250 residues. SABP binding domain polypeptides will consist of from about 50 to about 616 residues, preferably between about 75 and 300, more preferably between about 1 00 and about 250 residues. Particularly preferred polypeptides of the invention are those within the binding domain that are conserved between SABP and the EBL family. Residues within these conserved domains are shown in Figure 1, below. Two polynucleotides or polypeptides are said to be "identical" if the sequence of nucleotides or amino acid residues in the two sequences is the same when aligned for maximum correspondence. Optimal alignment of sequences for comparison may be conducted by the local homology algorithm of Smith and Waterman Adv. Appl . Math . 2: 482 (1981), by the homology alignment algorithm of Needleman and Wunsch J. Mol . Biol . 48:443 (1970), by the search for similarity method of Pearson and Lipman Proc. Natl . Acad. Sci . (U.S.A. ) 85: 2444 (1988) , by computerized implementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group, 575 Science Dr. , Madison, WI) , or by inspection. These references are incorporated herein by reference. The term "substantial identity" means that a polypeptide comprises a sequence that has at least 80% sequence identity, preferably 90%, more preferably 95% or more, compared to a reference sequence over a comparison window of about 20 residues to about 600 residues— typically about 50 to about 500 residues usually about 250 to 300 residues. The values of percent identity are determined using the programs above. Particularly preferred peptides of the present invention comprise a sequence in which at least 70% of the cysteine residues conserved in DABP and SABP are present. Additionally, the peptide will comprise a sequence in which at least 50% of the Tryptophan residues conserved in DABP and SABP are present. The term substantial similarity is also specifically defined here with respect to those amino acid residues found to be conserved between DABP, SABP and the sequences of the EBL family. These conserved amino acids consist prominently of tryptophan and cysteine residues conserved among all sequences reported here. In addition the conserved amino acid residues include phenylalanine residues which may be substituted with tyrosine. These amino acid residues may be determined to be conserved after the sequences have been aligned using methods outlined above by someone skilled in the art. Another indication that polypeptide sequences are substantially identical is if one protein is immunologically reactive with antibodies raised against the other protein. Thus, the polypeptides of the invention include polypeptides immunologically reactive with antibodies raised against the SABP binding domain, the DABP binding domain or raised against the conserved regions of the EBL family. Another indication that nucleotide sequences are substantially identical is if two molecules hybridize to each other under stringent conditions. Stringent conditions are sequence dependent and will be different in different circumstances. Generally, stringent conditions are selected to be about 5° C lower than the thermal melting point (Tm) for the specific sequence at a defined ionic strength and pH. The Tm is the temperature (under defined ionic strength and pH) at which 50% of the target sequence hybridizes to a perfectly matched probe. Typically, stringent conditions will be those in which the salt concentration is at least about 0.02 molar at pH 7 and the temperature is at least about 60°C. The phrases "isolated" or "biologically pure" refer to material which is substantially or essentially free from components which normally accompany it as found in its native state. Thus, the binding domain polypeptides of this invention do not contain materials normally associated with their in situ environment, e.g., other proteins from a merozoite membrane. However, even where a protein has been isolated to a homogenous or dominant band by PAGE, there can be trace contaminants in the range of 5-10% of native protein which co-purify with the desired protein. Isolated polypeptides of this invention do not contain such endogenous co-purified protein. Protein purity or homogeneity may be indicated by a number of means well known in the art, such as polyacrylamide gel electrophoresis of a protein sample, followed by visualization upon staining. For certain purposes high resolution will be needed and HPLC or a similar means for purification utilized. The term "residue" refers to an amino acid (D or L) or amino acid mimetic incorporated in a oligopeptide by an amide bond or amide bond mimetic. An amide bond mimetic of the invention includes peptide backbone modifications well known to those skilled in the art. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 represents an alignment of the predicted amino acid sequences of the DABP binding domain (Vivax) , the two homologous SABP domains (SABP Fl and SABP F2) and the sequenced members of the EBL gene family (ebl-el, E31a, EBL-e2 and the three homologous Proj3 domains. Figure 2 represents a schematic of the pRE4 cloning vector. Figure 3 shows primers useful for isolating sequences encoding the conserved motifs of the invention. DESCRIPTION OF THE PREFERRED EMBODIMENT The binding of merozoites and schizonts to erythrocytes is mediated by specific binding proteins on the surface of the merozoite or schizont and is necessary for erythrocyte invasion. In the case of P. falciparum , this binding involves specific interaction between sialic acid glycophorin residues on the erythrocyte and the sialic acid binding protein (SABP) on the surface of the merozoite or schizont. The ability of purified SABP to bind erythrocytes with chemically or enzy atically altered sialic acid residues paralleled the ability of P. falciparum to invade these erythrocytes. Furthermore, sialic acid deficient erythrocytes neither bind SABP nor support invasion by P. falciparum. The DNA encoding SABP from P . falciparum has also been cloned and sequenced. In P. vivax, specific binding to the erythrocytes involves interaction between the Duffy blood group antigen on the erythrocyte and the Duffy antigen binding protein (DABP) on the merozoite. Duffy binding proteins were defined biologically as those soluble proteins that appear in the culture supernatant after the infected erythrocytes release merozoites which bind to human Duffy positive, but not to human Duffy negative erythrocytes. It has been shown that binding of the P. vivax DABP protein to Duffy positive erythrocytes is blocked by antisera to the Duffy blood group determinants. Purified Duffy blood group antigens also block the binding to erythrocytes. DABP has also been shown to bind Duffy blood group determinants on Western blots. Duffy positive blood group determinants on human erythrocytes are essential for invasion of human erythrocytes by Plasmodium vivax. Both attachment and reorientation of P. vivax merozoites occur equally well on Duffy positive and negative erythrocytes. A junction then forms between the apical end of the merozoite and the Duffy-positive erythrocyte, followed by vacuole formation and entry of the merozoite into the vacuole. Junction formation and merozoite entry into the erythrocyte do not occur on Duffy negative cells, suggesting that the receptor specific for the Duffy determinant is involved in apical junction formation but not initial attachment. The DNA sequences encoding the DABP from P. vivax and P. knowlesi have been cloned and sequenced. P. vivax red cell invasion has an absolute requirement for the Duffy blood group antigen. Isolates of P. falcipa_ um , however, vary in their dependency on sialic acid for invasion. Certain P . falciparum clones have been developed which invade sialic acid deficient erythrocytes at normal rates. This suggests that certain strains of p. falciparum can interact with other ligands on the erythrocyte and so may possess multiple erythrocyte binding proteins with differing specificities. A basis for the present invention is the discovery of the binding domains in both DABP and SABP. Comparison of the predicted protein sequences of DABP and SABP reveals an amino-terminal, cysteine-rich region in both proteins with a high degree of similarity between the two proteins. The amino-terminal, cysteine-rich region of DABP contains about 325 amino acids, whereas the amino-terminal, cysteine-rich region of SABP contains about 616 amino acids. This is due to an apparent duplication of the amino-terminal, cysteine-rich region in the SABP protein. The cysteine residues are conserved between the two regions of SABP and DABP, as are the amino acids surrounding the cysteine residues and a number of aromatic amino acid residues in this region. The amino-terminal cysteine rich region and another cysteine-rich region near the carboxy1-terminus show the most similarity between the DABP and SABP proteins. The region of the amino acid sequence between these two cysteine-rich regions show only limited similarity between DABP and SABP. Other P. falciparum open reading frames and genes with regions that have substantial identity to binding domains of SABP and DABP have been identified. Multiple copies of these sequences exist in the parasite genome, indicating their important activity in host-parasite interactions. A family of these sequences (the EBL family) have been cloned from chromosome 7 subsegment libraries that were constructed during genetic studies of the chloroquine resistance locus (Wellems et. al . , PNAS 88: 3382-3386 (1991)). Alignment of EBL sequences identified domains highly conserved with the P. falciparum 175 kD protein; these conserved domains have in turn been used to identify genes (ebl-el, ebl-e2) one of which (ebl-el) resides on chromosome 13. Genetic linkage studies have placed this gene within a region of chromosome 13 that affects invasion of malarial parasites in human red blood cells (Wellems et al . , Cell 49:633-642 (1987)). Southern hybridization experiments using probes from these open reading frames have indicated that additional copies of these conserved sequences are located elsewhere in the genome. The largest of the open reading frames on chromosome 7 is 8 kilobases and contains four tandem repeats homologous to the N-terminal, cysteine-rich unit of SABP and DABP. Figure 1 represents an alignment of the EBL family with the DABP binding domain and two homologous regions of SABP (F χ and F 2 ) . The EBL family is divided into two sub-families to achieve optimal alignment. Conserved cysteine residues are shown in bold face and conserved aromatic residues are underlined. The polypeptides of the invention can be used to raise monoclonal antibodies specific for the binding domains of SABP, DABP or the conserved regions in the EBL gene family. The antibodies can be used for diagnosis of malarial infection or as therapeutic agents to inhibit binding of merozoites to erythrocytes. The production of monoclonal antibodies against a desired antigen is well known to those of skill in the art and is not reviewed in detail here. The multitude of techniques available to those skilled in the art for production and manipulation of various immunoglobulin molecules can thus be readily applied to inhibit binding. As used herein, the terms "immunoglobulin" and "antibody" refer to a protein consisting of one or more polypeptides substantially encoded by immunoglobulin genes. Immunoglobulins may exist in a variety of forms besides antibodies, including for example, Fv, Fab, and F(ab) 2 , as well as in single chains. For a general review of immunoglobulin structure and function see, Fundamental Immunology, 2d Ed., W.E. Paul ed. , Ravens Press, N.Y., (1989). Antibodies which bind polypeptides of the invention may be produced by a variety of means. The production of non-human monoclonal antibodies, e.g., murine, lagomorpha, equine, etc. , is well known and may be accomplished by, for example, immunizing the animal with a preparation containing the polypeptide. Antibody-producing cells obtained from the immunized animals are immortalized and screened, or screened first for the production of antibody which inhibits binding between and meroxoites and erythrocytes and then immortalized. For a discussion of general procedures of monoclonal antibody production see Harlow and Lane, Antibodies, A Laboratory Manual Cold Spring Harbor Publications, N.Y. (1988). Thus, the present invention allows targeting of protective immune responses or monoclonal antibodies to sequences in the binding domains that are conserved between SABP, DABP and encoded regions of the EBL family. Identification of the binding regions of these proteins facilitates vaccine development because it allows for a focus of effort upon the functional elements of the large molecules. The particular sequences within the binding regions refine the target to critical regions that have been conserved during evolution, and are thus preferred for use as vaccines against the parasite. The genes of the EBL family (which have not previously been sequenced) can be used as markers to detect the presence of the P. falciparum parasite in patients. This can be accomplished by means well known to practitioners in the art using tissue or blood from symptomatic patients in PCR reactions with oligonucleotides complementary to portions of the genes of the EBL family. Furthermore, sequencing the EBL family provides a means for skilled practitioners to generate defined probes to be used as genetic markers in a variety of applications. Additionally, the present invention defines a conserved motif present in, but not restricted to other members of the subphylum Apicomplexa which participates in host parasite interaction. This motif can be identified in Plasmodium species and other parasitic protozoa by the polymerase chain reaction using the synthetic oligonucleotide primers shown in Figure 3. PCR methods are described in detail below. These primers are designed from regions in the conserved motif showing the highest degree of conservation among DABP, SABP and the EBL family. Figure 3 shows these regions and the consensus amino acid sequences derived from them. A. General Methods Much of the nomenclature and general laboratory procedures required in this application can be found in Sambrook, et al . , Molecular Cloning A Laboratory Manual (2nd Ed.), Vol. 1-3, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, 1989. The manual is hereinafter referred to as "Sambrook, et al . " B. Methods for isolating DNA encoding SABP. DABP and EBL binding regions The nucleic acid compositions of this invention, whether RNA, cDNA, genomic DNA, or a hybrid of the various combinations, may be isolated from natural sources or may be synthesized in vitro. The nucleic acids claimed may be present in transformed or transfected whole cells, in a transformed or transfected cell lysate, or in a partially purified or substantially pure form. Techniques for nucleic acid manipulation of genes encoding the binding domains of the invention, such as subcloning nucleic acid sequences encoding polypeptides into expression vectors, labelling probes, DNA hybridization, and the like are described generally in Sambrook et al . , incorporated herein by reference. Recombinant DNA techniques can be used to produce the binding domain polypeptides. In general, the DNA encoding the SABP and DABP binding domains are first cloned or isolated in a form suitable for ligation into an expression vector. After ligation, the vectors containing the DNA fragments or inserts are introduced into a suitable host cell for expression of the recombinant binding domains. The polypeptides are then isolated from the host cells. There are various methods of isolating the DNA sequences encoding the SABP, DABP and EBL binding domains. Typically, the DNA is isolated from a genomic or cDNA library using labelled oligonucleotide probes specific for sequences in the DNA. Restriction endonuclease digestion of genomic DNA or cDNA containing the appropriate genes can be used to isolate the DNA encoding the binding domains of these proteins. Since the DNA sequences of the SABP and DABP genes are known, a panel of restriction endonucleases can be constructed to give cleavage of the DNA in the desired regions. After restriction endonuclease digestion, DNA encoding SABP binding domain or DABP binding domain is identified by its ability to hybridize with nucleic acid probes, for example on Southern blots, and these DNA regions are isolated by standard methods familiar to those of skill in the art. See Sambrook, et al . The polymerase chain reaction can also be used to prepare DABP, SABP EBL binding domain DNA. Polymerase chain reaction technology (PCR) is used to amplify nucleic acid sequences of the DABP and SABP binding domains directly from mRNA, from cDNA, and from genomic libraries or cDNA libraries. The primers shown in Figure 3 are particularly preferred for this process. Appropriate primers and probes for amplifying the SABP and DABP binding region DNA's are generated from analysis of the DNA sequences. In brief, oligonucleotide primers complementary to the two 3 • borders of the DNA region to be amplified are synthesized. The polymerase chain reaction is then carried out using the two primers. See PCR Protocols: A Guide to Methods and Applications . (Innis, M, Gelfand, D. , Sninsky, J. and White, T. , eds.). Academic Press, San Diego (1990) . Primers can be selected to amplify the entire DABP regions or to amplify smaller segments of the DABP and SABP binding domains, as desired. Oligonucleotides for use as probes are chemically synthesized according to the solid phase phosphoramidite triester method first described by Beaucage, S.L. and Caruthers, M.H., 1981, Tetrahedron Letts., 22(20) :1859-1862 using an automated synthesizer, as described in Needham-VanDevanter, D.R. , et al . 1984, Nucleic Acids Res., 12:6159-6168. Purification of oligonucleotides is by either native acrylamide gel electrophoresis or by anion-exchange HPLC as described in Pearson, J.D. and Regnier, F.E., 1983, J. Chrom. , 255:137-149. The sequence of the synthetic oligonucleotides can be verified using the chemical degradation method of Maxam, A.M. and Gilbert, 1980, in W. , Grossman, L. and Moldave, D., eds. Academic Press, New York, Methods in Enzymology, 65:499-560. Other methods known to those of skill in the art may also be used to isolate DNA encoding all or part of the SABP or DABP binding domains. See Sambrook, et al . C. Expression of DABP, SABP and EBL Binding Domain Polypeptides Once the binding domain DNAs are isolated and cloned, one may express the desired polypeptides in a recombinantly engineered cell such as bacteria, yeast, insect (especially employing baculoviral vectors) , and mammalian cells. It is expected that those of skill in the art are knowledgeable in the numerous expression systems available for expression of the DNA encoding the DABP and SABP binding domains. No attempt to describe in detail the various methods known for the expression of proteins in prokaryotes or eukaryotes will be made. In brief summary, the expression of natural or synthetic nucleic acids encoding binding domains will typically be achieved by operably linking the DNA or CDNA to a promoter (which is either constitutive or inducible) , followed by incorporation into an expression vector. The vectors can be suitable for replication and integration in either prokaryotes or eukaryotes. Typical expression vectors contain transcription and translation terminators, initiation sequences, and promoters useful for regulation of the expression of the DNA encoding the binding domains. To obtain high level expression of a cloned gene, it is desirable to construct expression plasmids which contain, at the minimum, a strong promoter to direct transcription, a ribosome binding site for translational initiation, and a transcription/translation terminator. 1. Expression in Prokaryotes Examples of regulatory regions suitable for this purpose in E. coli are the promoter and operator region of the E. coli tryptophan biosynthetic pathway as described by Yanofsky, C. , 1984, J. Bacteriol., 158:1018-1024 and the leftward promoter of phage lambda (P L ) as described by Herskowitz, I. and Hagen, D. , 1980, Ann. Rev. Genet., 14:399-445. The inclusion of selection markers in DNA vectors transformed in E. coli is also useful. Examples of such markers include genes specifying resistance to ampicillin, tetracycline, or chloramphenicol. See Sambrook et al . for details concerning selection markers for use in E. coli . The vector is selected to allow introduction into the appropriate host cell. Bacterial vectors are typically of plasmid or phage origin. Appropriate bacterial cells are infected with phage vector particles or transfected with naked phage vector DNA. If a plasmid vector is used, the bacterial cells are transfected with the plasmid vector DNA. Expression systems for expressing the DABP and SABP binding domains are available using E. coli. Bacillus, sp. (Palva, I et al . , 1983, Gene 22:229-235; Mosbach, K. et al . Nature, 302:543-545 and Salmonella . E. coli systems are preferred. The binding domain polypeptides produced by prokaryote cells may not necessarily fold properly. During purification from E. coli , the expressed polypeptides may first be denatured and then renatured. This can be accomplished by solubilizing the bacterially produced proteins in a chaotropic agent such as guanidine HCl and reducing all the cysteine residues with a reducing agent such as beta-mercaptoethanol. The polypeptides are then renatured, either by slow dialysis or by gel filtration. U.S. Patent No. 4,511,503. Detection of the expressed antigen is achieved by methods known in the art as radioimmunoassays. Western blotting techniques or immunoprecipitation. Purification from E. coli can be achieved following procedures described in U.S. Patent No. 4,511,503. 2. Synthesis of SABP. DABP and EBL Binding Domains in Eukaryotes A variety of eukaryotic expression systems such as yeast, insect cell lines and mammalian cells, are known to those of skill in the art. As explained briefly below, the DABP and SABP binding domains may also be expressed in these eukaryotic systems. a. Expression in Yeast Synthesis of heterologous proteins in yeast is well known and described. Methods in Yeast Genetics, Sherman, F. , et al . , Cold Spring Harbor Laboratory, (1982) is a well recognized work describing the various methods available to produce the binding domains in yeast. Examples of promoters for use in yeast include GAL1,10 (Johnson, M. , and Davies, R.W., 1984, Mol. and Cell. Biol., 4:1440-1448) ADH2 (Russell, D. , et al . 1983, J. Biol. Chem., 258:2674-2682), PH05 (EMBO J. 6:675-680, 1982), and MFαl (Herskowitz, I. and Oshima, Y., 1982, in The Molecular Biology of the Yeast Saccharomyces, (eds. Strathern, J.N. Jones, E.W. , and Broach, J.R. , Cold Spring Harbor Lab., Cold Spring Harbor, N.Y., pp. 181-209. A multicopy plasmid with a selective marker such as Leu-2, URA-3, Trp-1, and His-3 is also desirable. A number of yeast expression plasmids like YEp6, YEpl3, YEp4 can be used as vectors. A gene of interest can be fused to any of the promoters in various yeast vectors. The above-mentioned plasmids have been fully described in the literature (Botstein, et al . , ISIS , Gene, 8:17-24; Broach, et al . , 1979, Gene, 8:121-133). Two procedures are used in transforming yeast cells. In one case, yeast cells are first converted into protoplasts using zymolyase, lyticase or glusulase, followed by addition of DNA and polyethylene glycol (PEG) . The PEG-treated protoplasts are then regenerated in a 3% agar medium under selective conditions. Details of this procedure are given in the papers by J.D. Beggs, 1978, Nature (London), 275:104-109; and Hinnen, A., et al . , 1978, Proc. Natl. Acad. Sci. USA, 75:1929-1933. The second procedure does not involve removal of the cell wall. Instead the cells are treated with lithium chloride or acetate and PEG and put on selective plates (Ito r H., et al . , 1983, J. Bact., 153:163-168). The binding domains can be isolated from yeast by lysing the cells and applying standard protein isolation techniques to the lysates. The monitoring of the purification process can be accomplished by using Western blot techniques or radioimmunoassays of other standard immunoassay techniques. b. Expression in Mammalian and Insect Cell Cultures Illustrative of cell cultures useful for the production of the binding domains are cells of insect or mammalian origin. Mammalian cell systems often will be in the form of onolayers of cells although mammalian cell suspensions may also be used. Illustrative examples of mammalian cell lines include VERO and HeLa cells, Chinese hamster ovary (CHO) cell lines, W138, BHK, Cos-7 or MDCK cell lines. As indicated above, the vector, e. g. , a plasmid, which is used to transform the host cell, preferably contains DNA sequences to initiate transcription and sequences to control the translation of the antigen gene sequence. These sequences are referred to as expression control sequences. When the host cell is of insect or mammalian origin illustrative expression control sequences are obtained from the SV-40 promoter (Science, 222:524-527, 1983), the CMV I.E. Promoter (Proc. Natl. Acad. Sci. 81:659-663, 1984) or the metallothionein promoter (Nature 296:39-42, 1982). The cloning vector containing the expression control sequences is cleaved using restriction enzymes and adjusted in size as necessary or desirable and ligated with DNA coding for the SABP or DABP polypeptides by means well known in the art. As with yeast, when higher animal host cells are employed, polyadenlyation or transcription terminator sequences from known mammalian genes need to be incorporated into the vector. An example of a terminator sequence is the polyadenlyation sequence from the bovine growth hormone gene. Sequences for accurate splicing of the transcript may also be included. An example of a splicing sequence is the VP1 intron from SV40 (Sprague, J. et al . , 1983, J. Virol. 45: 773-781). Additionally, gene sequences to control replication in the host cell may be incorporated into the vector such as those found in bovine papilloma virus type-vectors. Saveria-Campo , M. , 1985, "Bovine Papilloma virus DNA a Eukaryotic Cloning Vector" in DNA Cloning Vol. II a Practical Approach Ed. D.M. Glover, IRL Press, Arlington, Virginia pp. 213-238. The host cells are competent or rendered competent for transformation by various means. There are several well-known methods of introducing DNA into animal cells. These include: calcium phosphate precipitation, fusion of the recipient cells with bacterial protoplasts containing the DNA, treatment of the recipient cells with liposomes containing the DNA, DEAE dextran, electroporation and micro-injection of the DNA directly into the cells. The transformed cells are cultured by means well known in the art. Biochemical Methods in Cell Culture and Virology, Kuchler, R.J., Dowden, Hutchinson and Ross, Inc., (1977) . The expressed DABP and SABP binding domain polypeptides are isolated from cells grown as suspensions or as monolayers. The latter are recovered by well known mechanical, chemical or enzymatic means. c. Expression in recombinant vaccinia virus- or adenovirus-infected cells In addition to use in recombinant expression systems, the isolated binding domain DNA sequences can also be used to transform viruses that transfect host cells in the patient. Live attenuated viruses, such as vaccinia or adenovirus, are convenient alternatives for vaccines because they are inexpensive to produce and are easily transported and administered. Vaccinia vectors and methods useful in immunization protocols are described, for example, in U.S. Patent No. 4,722,848, incorporated herein by reference. Suitable viruses for use in the present invention include, but are not limited to, pox viruses, such as canarypox and cowpox viruses, and vaccinia viruses, alpha viruses, adenoviruses, and other animal viruses. The recombinant viruses can be produced by methods well known in the art, for example, using homologous recombination or ligating two plasmids. A recombinant canarypox or cowpox virus can be made, for example, by inserting the DNA's encoding the DABP and SABP binding domain polypeptides into plasmids so that they are flanked by viral sequences on both sides. The DNA's encoding the binding domains are then inserted into the virus genome through homologous recombination. A recombinant adenovirus can be produced, for example, by ligating together two plasmids each containing about 50% of the viral sequence and the DNA sequence encoding erythrocyte binding domain polypeptide. Recombinant RNA viruses such as the alpha virus can be made via a CDNA intermediate using methods known in the art. In the case of vaccinia virus (for example, strain WR) , the DNA sequence encoding the binding domains can be inserted in the genome by a number of methods including homologous recombination using a transfer vector, pTKgpt-OFIS as described in Kaslow, et al . , Science 252 :1310-1313 (1991), which is incorporated herein by reference. Alternately the DNA encoding the SABP and DABP binding domains may be inserted into another plasmid designed for producing recombinant vaccinia, such as pGS62, Langford, C.L., et al . , 1986, Mol . Cell . Biol . 6:3191-3199. This plasmid consists of a cloning site for insertion of foreign genes, the P7.5 promoter of vaccinia to direct synthesis of the inserted gene, and the vaccinia TK gene flanking both ends of the foreign gene. Confirmation of production of recombinant virus can be achieved by DNA hybridization using CDNA encoding the DABP and SABP binding domain polypeptides and by immunodetection techniques using antibodies specific for the expressed binding domain polypeptides. Virus stocks may be prepared by infection of cells such as HELA S3 spinner cells and harvesting of virus progeny. The recombinant virus of the present invention-can be used to induce anti-SABP and anti-DABP binding domain antibodies in mammals, such as mice or humans. In addition, the recombinant virus can be used to produce the SABP and DABP binding domains by infecting host cells in vitro, which in turn express the polypeptide (see section on expression of SABP and DABP binding domains in eukaryotic cells, above). The present invention also relates to host cells infected with the recombinant virus. The host cells of the present invention are preferably mammalian, such as BSC-l cells. Host cells infected with the recombinant virus express the DABP and SABP binding domains on their cell surfaces. In addition, membrane extracts of the infected cells induce protective antibodies when used to inoculate or boost previously inoculated mammals. D. Purification of the SABP. DABP and EBL Binding Domain Polypeptides The binding domain polypeptides produced by recombinant DNA technology may be purified by standard techniques well known to those of skill in the art. Recombinantly produced binding domain polypeptides can be directly expressed or expressed as a fusion protein. The protein is then purified by a combination of cell lysis (e. g. , sonication) and affinity chromatography. For fusion products, subsequent digestion of the fusion protein with an appropriate proteolytic enzyme release the desired SABP and DABP binding domains. The polypeptides of this invention may be purified to substantial purity by standard techniques well known in the art, including selective precipitation with such substances as ammonium sulfate, column chromatography, immunopurification methods, and others. See, for instance, R. Scopes, Protein Purification : Principles and Practice, Springer-Verlag: New York (1982) , incorporated herein by reference. E. Production of Binding Domains by protein chemistry technigues The polypeptides of the invention can be synthetically prepared in a wide variety of ways. For instance polypeptides of relatively short size, can be synthesized in solution or on a solid support in accordance with conventional techniques. Various automatic synthesizers are commercially available and can be used in accordance with known protocols. See, for example, Stewart and Young, Solid Phase Peptide Synthesis, 2d. ed. , Pierce Chemical Co. (1984 ) . Alternatively, purified and isolated SABP, DABP or EBL family proteins may be treated with proteolytic enzymes in order to produce the binding domain polypeptides. For example, recombinant DABP and SABP proteins may be used for this purpose. The DABP and SABP protein sequence may then be analyzed to select proteolytic enzymes to be used to generate polypeptides containing desired regions of the DABP and SABP binding domain. The desired polypeptides are then purified by using standard techniques for protein and peptide purification. For a review of standard techniques see. Methods in Enzymology, "Guide to Protein Purification", M. Deutscher, ed. Vol. 182 (1990), pages 619-626, which is incorporated herein by reference. F. Modification of nucleic acid and polypeptide sequences The nucleotide sequences used to transfect the host cells used for production of recombinant binding domain polypeptides can be modified according to standard techniques to yield binding domain polypeptides, with a variety of desired properties. The binding domain polypeptides of the present invention can be readily designed and manufactured utilizing various recombinant DNA techniques well known to those skilled in the art. For example, the binding domain polypeptides can vary from the naturally-occurring sequence at the primary structure level by amino acid insertions, substitutions, deletions, and the like. These modifications can be used in a number of combinations to produce the final modified protein chain. The amino acid sequence variants can be prepared with various objectives in mind, including facilitating purification and preparation of the recombinant polypeptides. The modified polypeptides are also useful for modifying plasma half-life, improving therapeutic efficacy, and lessening the severity or occurrence of side effects during therapeutic use. The amino acid sequence variants are usually predetermined variants not found in nature but exhibit the same immunogenic activity as naturally occurring polypeptides. For instance, polypeptide fragments comprising only a portion (usually at least about 60-80%, typically 90-95%) of the primary structure may be produced. For use as vaccines, polypeptide fragments are typically preferred so long as at least one epitope capable of eliciting production of blocking antibodies remains. In general, modifications of the sequences encoding the binding domain polypeptides may be readily accomplished by a variety of well-known techniques, such as site-directed utagenesis (see, Giliman and Smith, Gene 8:81-97 (1979) and Roberts, S. et al . , Nature 328:731-734 (1987)). One of ordinary skill will appreciate that the effect of many mutations is difficult to predict. Thus, most modifications are evaluated by routine screening in a suitable assay for the desired characteristic. For instance, changes in the immunological character of the polypeptide can be detected by an appropriate competitive binding assay. Modifications of other properties such as redox or thermal stability, hydrophobicity, susceptibility to proteolysis, or the tendency to aggregate are all assayed according to standard techniques. G. Diagnostic and Screening Assays The polypeptides of the invention can be used in diagnostic applications for the detection of merozoites in a biological sample. The presence of parasites can be detected using several well recognized specific binding assays based on immunological results. (See U.S. Patents 4,366,241; 4,376,110; 4,517,288; and 4,837,168, which are hereby incorporated by reference.) For instance, labeled monoclonal antibodies to polypeptides of the invention can be used to detect merozoites in a biological sample. Alternatively, labelled polypeptides of the invention can be used to detect the presence of antibodies to SABP or DABP in a biological sample. For a review of the general procedures in diagnostic immunoassays, see also Basic and Clinical Immunology 7th Edition (D. Stites and A. Terr ed.) 1991, which is hereby incorporated by * reference. In addition, modified polypeptides, antibodies or other compounds capable of inhibiting the interaction between SABP or DABP and erythrocytes can be assayed for biological activity. For instance, polypeptides can be recombinantly expressed on the surface of cells and the ability of the cells to bind erythrocytes can be measured as described below. Alternatively, peptides or antibodies can tested for the ability to inhibit binding between erythrocytes and merozoites or SABP and DABP. Cell-free assays can also be used to measure binding of DABP or SABP polypeptides to isolated Duffy antigen or glycophorin polypeptides. For instance, the erythrocyte proteins can be immobilized on a solid surface and binding of labelled SABP or DABP polypeptides can be measured. Many assay formats employ labelled assay components. The labelling systems can be in a variety of forms. The label may be coupled directly or indirectly to the desired component of the assay according to methods well known in the art. A wide variety of labels may be used. The component may be labelled by any one of several methods. The most common method of detection is the use of autoradiography with 3 H, 125 I, 35 S, 14 C, or 32 P labelled compounds or the like. Non-radioactive labels include ligands which bind to labelled antibodies, fluorophores, chemiluminescent agents, enzymes, and antibodies which can serve as specific binding pair members for a labelled ligand. The choice of label depends on sensitivity required, ease of conjugation with the compound, stability requirements, and available instrumentation. In addition, the polypeptides of the invention can be assayed using animal models, well known to those of skill in the art. For P falciparum the in vivo models include Aotus sp. monkeys or chimpanzees; for P. vivax the in vivo models include Saimiri monkeys. H. Pharmaceutical compositions comprising binding domain polypeptides The polypeptides of the invention are useful in therapeutic and prophylactic applications for the treatment o f malaria. Pharmaceutical compositions of the invention are suitable for use in a variety of drug delivery systems. Suitable formulations for use in the present invention are found in Remington ' s Pharmaceutical Sciences, Mack Publishing Company, Philadelphia, PA, 17th ed. (1985), which is incorporated herein by reference. For a brief review of methods for drug delivery, see, Langer, Science 249:1 527-15 3 3 (1990) , which is incorporated herein by reference. The polypeptides of the present invention can be used in pharmaceutical and vaccine compositions that are useful for administration to mammals, particularly humans. The polypeptides can be administered together in certain circumstances, e . g. where infection by both P. falciparum and P. vivax is likely. Thus, a single pharmaceutical composition can be used for the treatment or prophylaxis of malaria caused by both parasites. The compositions are suitable for single administrations or a series of administrations. When given as a series, inoculations subsequent to the initial administration are given to boost the immune response and are typically referred to as booster inoculations. The pharmaceutical compositions of the invention are intended for parenteral, topical, oral or local administration. Preferably, the pharmaceutical compositions are administered parenterally, e . g. , intravenously, subcutaneously, intradermally, or intramuscularly. Thus, the invention provides compositions for parenteral administration that comprise a solution of the agents described above dissolved or suspended in an acceptable carrier, preferably an aqueous carrier. A variety of aqueous carriers may be used, e.gr., water, buffered water, 0.4% saline, 0.3% glycine, hyaluronic acid and the like. These compositions may be sterilized by conventional, well known sterilization techniques, or may be sterile filtered. The resulting aqueous solutions may be packaged for use as is, or lyophilized, the lyophilized preparation being combined with a sterile solution prior to administration. The compositions may contain pharmaceutically acceptable auxiliary substances as required to approximate physiological conditions, such as pH adjusting and buffering agents, tonicity adjusting agents, wetting agents and the like, for example, sodium acetate, sodium lactate, sodium chloride, potassium chloride, calcium chloride, sorbitan monolaurate, triethanolamine oleate, etc. For solid compositions, conventional nontoxic solid carriers may be used which include, for example, pharmaceutical grades of mannitol, lactose, starch, magnesium stearate, sodium saccharin, talcum, cellulose, glucose, sucrose, magnesium carbonate, and the like. For oral administration, a pharmaceutically acceptable nontoxic composition is formed by incorporating any of the normally employed excipients, such as those carriers previously listed, and generally 10-95% of active ingredient and more preferably at a concentration of 25%-75%. For aerosol administration, the polypeptides are preferably supplied in finely divided form along with a surfactant and propellant. The surfactant must, of course, be nontoxic, and preferably soluble in the propellant. Representative of such agents are the esters or partial esters of fatty acids containing from 6 to 22 carbon atoms, such as caproic, octanoic, lauric, palmitic, stearic, linoleic, linolenic, olesteric and oleic acids with an aliphatic polyhydric alcohol or its cyclic anhydride. Mixed esters, such as mixed or natural glycerides may be employed. A carrier can also be included, as desired, as with, e .g. , lecithin for intranasal delivery. In certain embodiments patients with malaria may be treated with SABP or DABP polypeptides or other specific blocking agents (e . g. monoclonal antibodies) that prevent binding of Plasmodium merozoites and schizonts to the erythrocyte surface. The amount administered to the patient will vary depending upon what is being administered, the state of the patient and the manner of administration. In therapeutic applications, compositions are administered to a patient already suffering from malaria in an amount sufficient to inhibit spread of the parasite through erythrocytes and thus cure or at least partially arrest the symptoms of the disease and its complications. An amount adequate to accomplish this is defined as "therapeutically effective dose." Amounts effective for this use will depend on the severity of the disease and the weight and general state of the patient. But will generally be in the range of about lmg to about 5gm per day, preferably about 100 mg per day, for a 70 kg patient. Alternatively, the polypeptides of the invention can be used prophylactically as vaccines. The vaccines of the invention contain as an active ingredient an immunogenically effective amount of the binding domain polypeptide or of a recombinant virus as described herein. The immune response may include the generation of antibodies; activation of cytotoxic T lymphocytes (CTL) against cells presenting peptides derived from the peptides encoded by the SABP, DABP or EBL sequences of the present invention, or other mechanisms well known in the art. See e . g. Paul Fundamental Immunology Second Edition published by Raven press New York (incorporated herein by reference) for a description of immune response. Useful carriers are well known in the art, and include, for example, thyroglobulin, albumins such as human serum albumin, tetanus toxoid, polyamino acids such as poly(D-lysine:D- glutamic acid) , influenza, hepatitis B virus core protein, hepatitis B virus recombinant vaccine. The vaccines can also contain a physiologically tolerable (acceptable) diluent such as water, phosphate buffered saline, or saline, and further typically include an adjuvant. Adjuvants such as incomplete Freund's adjuvant, aluminum phosphate, aluminum hydroxide, or alum are materials well known in the art. The DNA or RNA encoding the SABP or DABP binding domains and the EBL gene family motifs may be introduced into patients to obtain an immune response to the polypeptides which the nucleic acid encodes. Wolff et. al. , Science 247: 1465-1468 (1990) which is incorporated herein by reference describes the use of nucleic acids to produce expression of the genes which the nucleic acids encode. Vaccine compositions containing the polypeptides, nucleic acids or viruses of the invention are administered to a patient to elicit a protective immune response against the polypeptide. A "protective immune response" is one which prevents or inhibits the spread of the parasite through erythrocytes and thus at least partially prevent the symptoms of the disease and its complications. An amount sufficient to accomplish this is defined as an "immunogenically effective dose." Amounts effective for this use will depend on the composition, the manner of administration, the weight and general state of health of the patient, and the judgment of the prescribing physician. For peptide compositions, the general range for the initial immunization (that is for therapeutic or prophylactic administration) is from about 100 μg to about 1 gm of peptide for a 70 kg patient, followed by boosting dosages of from about 100 μg to about 1 gm of the polypeptide pursuant to a boosting regimen over weeks to months depending upon the patient's response and condition e.g. by measuring levels of parasite in the patient's blood. For nucleic acids, typically 30-lθθθug of nucleic acid is injected into a 70kg patient, more typically about 50-150ug of nucleic acid is injected into a 70kg patient followed by boosting doses as appropriate. The following example is offered by way of illustration, not by way of limitation. EXAMPLE Identification of the amino-terminal, cysteine-rich region of SABP and DABP as binding domains for erythrocytes 1. Expression of the SABP binding domain polypeptide on the surface of Cos cells. To demonstrate that the amino-terminal, cysteine-rich region of the SABP protein is the sialic acid binding region, this region of the protein was expressed on the surface of mammalian Cos cells in vitro . This DNA sequence is from position 1 to position 1848 of the SABP DNA sequence (SEQ ID No 3) . Polymerase chain reaction technology (PCR) was used to amplify this region of the SABP DNA directly from the cloned gene. Sequences corresponding to restriction endonuclease sites for Pvull or Apal were incorporated into the oligonucleotide sequence of the probes used in PCR amplification in order to facilitate insertion of the PCR-amplified regions into the pRE4 vector (see below) . The specific oligonucleotides, 5•-ATCGATCAGCTGGGAAGAAATACTTCATCT-3 • and 5 « -ATCGATGGGCCCCGAAGTTTGTTCATTATT-3 ' were synthesized. These oligonucleotides were used as primers to PCR-amplify the region of the DNA sequence encoding the cysteine-rich amino terminal region of the SABP protein. PCR conditions were based on the standard described in Saiki, et al. , Science 239: 487-491 (1988). Template DNA was provided from cloned fragments of the gene encoding SABP which had been spliced and re-cloned as a single open-reading frame piece. The vector, pRE4, used for expression in Cos cells is shown in Fig.l. The vector has an SV40 origin of replication, an ampicillin resistance marker and the Herpes simplex virus glycoprotein D gene (HSV glyd) cloned downstream of the Rous sarcoma virus long terminal repeats (RSV LTR) . Part of the extracellular domain of the HSV glyd gene was excised using the Pvull and Apal sites in HSV glyd. As described above, the PCR oligonucleotide primers contained the Pvull or Apal restriction sites. The PCR-amplified DNA fragments obtained above were digested with the restriction enzymes Pvull and Apal and cloned into the Pvull and Apal sites of the vector pRE4. These constructs were designed to express regions of the SABP protein as chimeric proteins with the signal sequence of HSV glyd at the N-terminal end and the transmembrane and cytoplasmic domain of HSV glyd at the C-terminal end. The signal sequence of HSV glyd targets these chimeric proteins to the surface of Cos cells and the transmembrane segment of HSV glyd anchors these chimeric proteins to the Cos cell surface. Mammalian Cos cells were transfected with the pRE4 constructs containing the PCR-amplified SABP DNA regions, by calcium phosphate precipitation according to standard techniques. 2. Expression of the DABP binding domain polypeptide on the surface of Cos cells. To demonstrate that the amino-terminal, cysteine-rich region of the DABP protein is the binding domain, this region was expressed on the surface of Cos cells. This region of the DNA sequence from position 1-975 was first PCR-amplified (SEQ ID No 1) . Sequences corresponding to restriction endonuclease sites for Pvull or Apal were incorporated into the oligonucleotide probes used for PCR amplification in order to facilitate subsequent insertion of the amplified DNA into the pRE4 vector, as described above. The oligonucleotides, 5'-TCTCGTCAGCTGACGATCTCTAGTGCTATT-3' and 5'-ACGAGTGGGCCCTGTCACAACTTCCTGAGT-3' were synthesized. These oligonucleotides were used as primers to amplify the region of the DABP DNA sequence encoding the cysteine-rich, amino-terminal region of the DABP protein directly from the cloned DABP gene, using the same conditions described above. The same pRE4 vector described above in the section on expression of SABP regions in Cos cells was also used as a _ vector for the DABP DNA regions. 3. Binding studies with erythrocytes. To demonstrate their ability to bind human erythrocytes, the transfected Cos cells expressing binding domains from DABP and SABP were incubated with erythrocytes for two hours at 37°C in culture media (DMEM/10% FBS) . The non-adherent erythrocytes were removed with five washes of phosphate-buffered saline and the bound erythrocytes were observed by light microscopy. Cos cells expressing the amino terminal, cysteine-rich SABP polypeptides on their surface bound untreated human erythrocytes, but did not bind neuraminidase treated erythrocytes, that is, erythrocytes which lack sialic acid residues on their surface (data not shown) . Cos cells expressing other regions of the SABP protein on their surface did not bind human erythrocytes (data not shown) . These results identified the amino-terminal, cysteine-rich region of SABP as the erythrocyte binding domain and indicated that the binding of Cos cells expressing these regions to human erythrocytes is specific. Furthermore, the binding of the expressed region to erythrocytes is identical to the binding pattern seen for the authentic SABP- 175 molecule upon binding to erythrocytes. Similarly, Cos cells expressing the amino-terminal cysteine-rich region of DABP on their surface bound Duffy-positive human erythrocytes, but did not bind Duffy-negative human erythrocytes, that is erythrocytes which lack the Duffy blood group antigen (data not shown) . Cos cells expressing other regions of the DABP protein on their surface did not bind human erythrocytes (data not shown) . These results identified the amino-terminal cysteine rich region of DABP as the erythrocyte binding domain and indicated that the binding of the Cos cells was specific. SEQUENCE LISTING (1) GENERAL INFORMATION: (i) APPLICANT: (A) NAME: The United States Of America, as represented by The Secretary of the Department of Health and Human Services (ii) TITLE OF INVENTION: BINDING DOMAINS FROM PLASMODIUM VIVAX AND PLASMODIUM FALCIPARUM ERYTHROCYTE BINDING PROTEINS (iii) NUMBER OF SEQUENCES: 12 (iv) COMPUTER READABLE FORM: (A) MEDIUM TYPE: Floppy disk (B) COMPUTER: IBM PC compatible (C) OPERATING SYSTEM: PC-DOS/MS-DOS (D) SOFTWARE: Patentin Release #1.0, Version #1.25 (v) CURRENT APPLICATION DATA: (A) APPLICATION NUMBER: WO not yet assigned (B) FILING DATE: 07-SEP-1994 (C) CLASSIFICATION: (vi) PRIOR APPLICATION DATA: (A) APPLICATION NUMBER: US 08/119,677 (B) FILING DATE: 10-SEP-1993 (viii) ATTORNEY/AGENT INFORMATION: (A) NAME: Bastian, Kevin L. (B) REGISTRATION NUMBER: 34,774 (C) REFERENCE/DOCKET NUMBER: 15280-139000 (ix) TELECOMMUNICATION INFORMATION: (A) TELEPHONE: (415) 543-9600 (B) TELEFAX: (415) 543-5043 (2) INFORMATION FOR SEQ ID NO:l: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4084 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (iii) HYPOTHETICAL: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Plasmodium vivax (xi) SEQUENCE DESCRIPTION: SEQ ID NO:l: AAGCTTTTAA AAATAGCAAC AAAATTTCGA AACATTGCCA CAAAAATTTT ATGTTTTACA 60 TATATTTAGA TTCATACAAT TTAGGTGTAC CCTGTTTTTT GATATATGCG CTTAAATTTT 120 TTTTTCGCTC ATATGTTTAG TTATATGTGT AGAACAACTT GCTGAATAAA TTACGTACAC 180 TTTCTGTTCT GAATAATATT ACCACATACA TTTAATTTTA AATACTATGA AAGGAAAAAA 240 CCGCTCTTTA TTTGTTCTCC TAGTTTTATT ATTGTTACAC AAGGTATCAT ATAAGGATGA 300 TTTTTCTATC ACACTAATAA ATTATCATGA AGGAAAAAAA TATTTAATTA TACTAAAAAG 360 AAAATTAGAA AAAGCTAAT ATCGTGATGT TTGCAATTTT TTTCTTCATT TCTCTCAGGT 420 AAATAATGTA TTATTAGAAC GAACAATTGA AACCCTTCTA GAATGCAAAA ATGAATATGT 480 GAAAGGTGAA AATGGTTATA AATTAGCTAA AGGACACCAC TGTGTTGAGG AAGATAACTT 540 AGAACGATGG TTACAAGGAA CCAATGAAAG AAGAAGTGAG GAAAATATAA AATATAAATA 600 TGGAGTAACG GAACTAAAAA TAAAGTATGC GCAAATGAAT GGAAAAAGAA GCAGCCGCAT 660 TTTGAAGGAA TCAATTTACG GGGCGCATAA CTTTGGAGGC AACAGTTACA TGGAGGGAAA 720 AGATGGAGGA GATAAAACTG GGGAGGAAAA AGATGGAGAA CATAAAACTG ATAGTAAAAC 780 TGATAACGGG AAAGGTGCAA ACAATTTGGT AATGTTAGAT TATGAGACAT CTAGCAATGG 840 CCAGCCAGCG GGAACCCTTG ATAATGTTCT TGAATTTGTG ACTGGGCATG AGGGAAATTC 900 TCGTAAAAAT TCCTCGAATG GTGGCAATCC TTACGATATT GATCATAAGA AAACGATCTC 960 TAGTGCTATT ATAAATCATG CTTTTCTTCA AAATACTGTA ATGAAAAACT GTAATTATAA 1020 GAGAAAACGT CGGGAAAGAG ATTGGGACTG TAACACTAAG AAGGATGTTT GTATACCAGA 1080 TCGAAGATAT CAATTATGTA TGAAGGAACT TACGAATTTG GTAAATAATA CAGACACAAA 1140 TTTTCATAGG GATATAACAT TTCGAAAATT ATATTTGAAA AGGAAACTTA TTTATGATGC 1200 TGCAGTAGAG GGCGATTTAT TACTTAAGTT GAATAACTAC AGATATAACA AAGACTTTTG 1260 CAAGGATATA AGATGGAGTT TGGGAGATTT TGGAGATATA ATTATGGGAA CGGATATGGA 1320 AGGCATCGGA TATTCCAAAG TAGTGGAAAA TAATTTGCGC AGCATCTTTG GAACTGATGA 1380 AAAGGCCCAA CAGCGTCGTA AACAGTGGTG GAATGAATCT AAAGCACAAA TTTGGACAGC 1440 AATGATGTAC TCAGTTAAAA AAAGATTAAA GGGGAATTTT ATATGGATTT GTAAATTAAA 1500 TGTTGCGGTA AATATAGAAC CGCAGATATA TAGATGGATT CGAGAATGGG GAAGGGATTA 1560 CGTGTCAGAA TTGCCCACAG AAGTGCAAAA ACTGAAAGAA AAATGTGATG GAAAAATCAA 1620 TTATACTGAT AAAAAAGTAT GTAAGGTACC ACCATGTCAA AATGCGTGTA AATCATATGA 1680 TCAATGGATA ACCAGAAAAA AAAATCAATG GGATGTTCTG TCAAATAAAT TCATAAGTGT 1740 AAAAAACGCA GAAAAGGTTC AGACGGCAGG TATCGTAACT CCTTATGATA TACTAAAACA 1800 GGAGTTAGAT GAATTTAACG AGGTGGCTTT TGAGAATGAA ATTAACAAAC GTGATGGTGC 1860 ATATATTGAG TTATGCGTTT GTTCCGTTGA AGAGGCTAAA AAAAATACTC AGGAAGTTGT 1920 GACAAATGTG GACAATGCTG CTAAATCTCA GGCCACCAAT TCAAATCCGA TAAGTCAGCC 1980 TGTAGATAGT AGTAAAGCGG AGAAGGTTCC AGGAGATTCT ACGCATGGAA ATGTTAACAG 2040 TGGCCAAGAT AGTTCTACCA CAGGTAAAGC TGTTACGGGG GATGGTCAAA ATGGAAATCA 2100 GACACCTGCA GAAAGCGATG TACAGCGAAG TGATATTGCC GAAAGTGTAA GTGCTAAAAA 2160 TGTTGATCCG CAGAAATCTG TAAGTAAAAG AAGTGACGAC ACTGCAAGCG TTACAGGTAT 2220 TGCCGAAGCT GGAAAGGAAA ACTTAGGCGC ATCAAATAGT CGACCTTCTG AGTCCACCGT 2280 TGAAGCAAAT AGCCCAGGTG ATGATACTGT GAACAGTGCA TCTATACCTG TAGTGAGTGG 2340 TGAAAACCCA TTGGTAACCC CCTATAATGG TTTGAGGCAT TCGAAAGACA ATAGTGATAG 2400 CGATGGACCT GCGGAATCAA TGGCGAATCC TGATTCAAAT AGTAAAGGTG AGACGGGAAA 2460 GGGGCAAGAT AATGATATGG CGAAGGCTAC TAAAGATAGT AGTAATAGTT CAGATGGTAC 2520 CAGCTCTGCT ACGGGTGATA CTACTGATGC AGTTGATAGG GAAATTAATA AAGGTGTTCC 2580 TGAGGATAGG GATAAAACTG TAGGAAGTAA AGATGGAGGG GGGGAAGATA ACTCTGCAAA 2640 TAAGGATGCA GCGACTGTAG TTGGTGAGGA TAGAATTCGT GAGAACAGCG CTGGTGGTAG 2700 CACTAATGAT AGATCAAAAA ATGACACGGA AAAGAACGGG GCCTCTACCC CTGACAGTAA 2760 ACAAAGTGAG GATGCAACTG CGCTAAGTAA AACCGAAAGT TTAGAATCAA CAGAAAGTGG 2820 AGATAGAACT ACTAATGATA CAACTAACAG TTTAGAAAAT AAAAATGGAG GAAAAGAAAA 2880 GGATTTACAA AAGCATGATT TTAAAAGTAA TGATACGCCG AATGAAGAAC CAAATTCTGA 2940 TCAAACTACA GATGCAGAAG GACATGACAG GGATAGCATC AAAAATGATA AAGCAGAAAG 3000 GAGAAAGCAT ATGAATAAAG ATACTTTTAC GAAAAATACA AATAGTCACC ATTTAAATAG 3060 TAATAATAAT TTGAGTAATG GAAAATTAGA TATAAAAGAA TACAAATACA GAGATGTCAA 3120 AGCAACAAGG GAAGATATTA TATTAATGTC TTCAGTACGC AAGTGCAACA ATAATATTTC 3180 TTTAGAGTAC TGTAACTCTG TAGAGGACAA AATATCATCG AATACTTGTT CTAGAGAGAA 3240 AAGTAAAAAT TTATGTTGCT CAATATCGGA TTTTTGTTTG AACTATTTTG ACGTGTATTC 3300 TTATGAGTAT CTTAGCTGCA TGAAAAAGGA ATTTGAAGAT CCATCCTACA AGTGCTTTAC 3360 GAAAGGGGGC TTTAAAGGTA TGCAGAAAAA GATGCTGAAT AGAGAAAGGT GTTGAGTAAA 3420 TTAAAAAGGA ATTAATTTTA GGAATGTTAT AAACATTTTT GTACCCAAAA TTCTTTTTGC 3480 AGACAAGACT TACTTTGCCG CGGCGGGAGC GTTGCTGATA CTGCTGTTGT TAATTGCTTC 3540 AAGGAAGATG ATCAAAAATG AGTAACCAGA AAATAAAATA AAATAACATA AAATAAAATA 3600 AAAACTAGAA TAACAATTAA AATAAAATAA AATGAGAAAT GCCTGTTAAT GCACAGTTAA 3660 TTCTAACGAT TCCATTTGTG AAGTTTTAAA GAGAGCACAA ATGCATAGTC ATTATGTCCA 3720 TGCATATATA CACATATATG TACGTATATA TAATAAACGC ACACTTTCTT GTTCGTACAG 3780 TTCTGAAGAA GCTACATTTA ATGAGTTTGA AGAATACTGT GATAATATTC ACAGAATCCC 3840 TCTGATGCCT AACAGTAATT CAAATTTCAA GAGCAAAATT CCATTTAAAA AGAAATGTTA 3900 CATCATTTTG CGTTTTTCTT TTTTTCTTTT TTTTTTCTTT TTTAGATATT GAACACATGC 3960 AGCCATCAAC CCCCCTGGAT TATTCATGAT GCTACTTTGG TAAGTAAAAG CAATTCTGAT 4020 TGTAGTGCTG ATGTAATTTT AGTCATTTTG CTTGCTGCAA TAAACGAGAA AATATATCAA 4080 GCTT 4084 (2) INFORMATION FOR SEQ ID NO:2: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1115 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Plasmodium vivax (xi) SEQUENCE DESCRIPTION: SEQ ID NO:2: Met Lys Gly Lys Asn Arg Ser Leu Phe Val Leu Leu Val Leu Leu Leu 1 5 10 15 Leu His Lys Val Ser Tyr Lys Asp Asp Phe Ser lie Thr Leu lie Asn 20 25 30 Tyr His Glu Gly Lys Lys Tyr Leu lie lie Leu Lys Arg Lys Leu Glu 35 40 45 Lys Ala Asn Asn Arg Asp Val Cys Asn Phe Phe Leu His Phe Ser Gin 50 55 60 Val Asn Asn Val Leu Leu Glu Arg Thr lie Glu Thr Leu Leu Glu Cys 65 70 75 80 Lys Asn Glu Tyr Val Lys Gly Glu Asn Gly Tyr Lys Leu Ala Lys Gly 85 90 95 His His Cys Val Glu Glu Asp Asn Leu Glu Arg Trp Leu Gin Gly Thr 100 105 110 Asn Glu Arg Arg Ser Glu Glu Asn lie Lys Tyr Lys Tyr Gly Val Thr 115 120 125 Glu Leu Lys lie Lys Tyr Ala Gin Met Asn Gly Lys Arg Ser Ser Arg 130 135 140 lie Leu Lys Glu Ser lie Tyr Gly Ala His Asn Phe Gly Gly Asn Ser 145 150 155 160 Tyr Met Glu Gly Lys Asp Gly Gly Asp Lys Thr Gly Glu Glu Lys Asp 165 170 175 Gly Glu His Lys Thr Asp Ser Lys Thr Asp Asn Gly Lys Gly Ala Asn 180 185 190 Asn Leu Val Met Leu Asp Tyr Glu Thr Ser Ser Asn Gly Gin Pro Ala 195 200 205 Gly Thr Leu Asp Asn Val Leu Glu Phe Val Thr Gly His Glu Gly Asn 210 215 220 Ser Arg Lys Asn Ser Ser Asn Gly Gly Asn Pro Tyr Asp lie Asp His 225 230 235 240 Lys Lys Thr lie Ser Ser Ala lie lie Asn His Ala Phe Leu Gin Asn 245 250 255 Thr Val Met Lys Asn Cys Asn Tyr Lys Arg Lys Arg Arg Glu Arg Asp 260 265 270 Trp Asp Cys Asn Thr Lys Lys Asp Val Cys lie Pro Asp Arg Arg Tyr 275 280 285 Gin Leu Cys Met Lys Glu Leu Thr Asn Leu Val Asn Asn Thr Asp Thr 290 295 300 Asn Phe His Arg Asp lie Thr Phe Arg Lys Leu Tyr Leu Lys Arg Lys 305 310 315 320 Leu lie Tyr Asp Ala Ala Val Glu Gly Asp Leu Leu Leu Lys Leu Asn 325 330 335 Asn Tyr Arg Tyr Asn Lys Asp Phe Cys Lys Asp lie Arg Trp Ser Leu 340 345 350 Gly Asp Phe Gly Asp lie lie Met Gly Thr Asp Met Glu Gly lie Gly 355 360 365 Tyr Ser Lys Val Val Glu Asn Asn Leu Arg Ser lie Phe Gly Thr Asp 370 375 380 Glu Lys Ala Gin Gin Arg Arg Lys Gin Trp Trp Asn Glu Ser Lys Ala 385 390 395 400 Gin lie Trp Thr Ala Met Met Tyr Ser Val Lys Lys Arg Leu Lys Gly 405 410 415 Asn Phe lie Trp lie Cys Lys Leu Asn Val Ala Val Asn lie Glu Pro 420 425 430 Gin lie Tyr Arg Trp lie Arg Glu Trp Gly Arg Asp Tyr Val Ser Glu 435 440 445 Leu Pro Thr Glu Val Gin Lys Leu Lys Glu Lys Cys Asp Gly Lys lie 450 455 460 Asn Tyr Thr Asp Lys Lys Val Cys Lys Val Pro Pro Cys Gin Asn Ala 465 470 475 480 Cys Lys Ser Tyr Asp Gin Trp lie Thr Arg Lys Lys Asn Gin Trp Asp 485 490 495 Val Leu Ser Asn Lys Phe lie Ser Val Lys Asn Ala Glu Lys Val Gin 500 505 510 Thr Ala Gly lie Val Thr Pro Tyr Asp lie Leu Lys Gin Glu Leu Asp 515 520 525 Glu Phe Asn Glu Val Ala Phe Glu Asn Glu lie Asn Lys Arg Asp Gly 530 535 540 Ala Tyr lie Glu Leu Cys Val Cys Ser Val Glu Glu Ala Lys Lys Asn 545 550 555 560 Thr Gin Glu Val Val Thr Asn Val Asp Asn Ala Ala Lys Ser Gin Ala 565 570 575 Thr Asn Ser Asn Pro lie Ser Gin Pro Val Asp Ser Ser Lys Ala Glu 580 585 590 Lys Val Pro Gly Asp Ser Thr His Gly Asn Val Asn Ser Gly Gin Asp 595 600 605 Ser Ser Thr Thr Gly Lys Ala Val Thr Gly Asp Gly Gin Asn Gly Asn 610 615 620 Gin Thr Pro Ala Glu Ser Asp Val Gin Arg Ser Asp lie Ala Glu Ser 625 630 635 640 Val Ser Ala Lys Asn Val Asp Pro Gin Lys Ser Val Ser Lys Arg Ser 645 650 655 Asp Asp Thr Ala Ser Val Thr Gly lie Ala Glu Ala Gly Lys Glu Asn 660 665 670 Leu Gly Ala Ser Asn Ser Arg Pro Ser Glu Ser Thr Val Glu Ala Asn 675 680 685 Ser Pro Gly Asp Asp Thr Val Asn Ser Ala Ser lie Pro Val Val Ser 690 695 700 Gly Glu Asn Pro Leu Val Thr Pro Tyr Asn Gly Leu Arg His Ser Lys 705 710 715 720 Asp Asn Ser Asp Ser Asp Gly Pro Ala Glu Ser Met Ala Asn Pro Asp 725 730 735 Ser Asn Ser Lys Gly Glu Thr Gly Lys Gly Gin Asp Asn Asp Met Ala 740 745 750 Lys Ala Thr Lys Asp Ser Ser Asn Ser Ser Asp Gly Thr Ser Ser Ala 755 760 765 Thr Gly Asp Thr Thr Asp Ala Val Asp Arg Glu lie Asn Lys Gly Val 770 775 780 Pro Glu Asp Arg Asp Lys Thr Val Gly Ser Lys Asp Gly Gly Gly Glu 785 790 795 800 Asp Asn Ser Ala Asn Lys Asp Ala Ala Thr Val Val Gly Glu Asp Arg 805 810 815 lie Arg Glu Asn Ser Ala Gly Gly Ser Thr Asn Asp Arg Ser Lys Asn 820 825 830 Asp Thr Glu Lys Asn Gly Ala Ser Thr Pro Asp Ser Lys Gin Ser Glu 835 840 845 Asp Ala Thr Ala Leu Ser Lys Thr Glu Ser Leu Glu Ser Thr Glu Ser 850 855 860 Gly Asp Arg Thr Thr Asn Asp Thr Thr Asn Ser Leu Glu Asn Lys Asn 865 870 875 880 Gly Gly Lys Glu Lys Asp Leu Gin Lys His Asp Phe Lys Ser Asn Asp 885 890 895 Thr Pro Asn Glu Glu Pro Asn Ser Asp Gin Thr Thr Asp Ala Glu Gly 900 905 910 His Asp Arg Asp Ser lie Lys Asn Asp Lys Ala Glu Arg Arg Lys His 915 920 925 Met Asn Lys Asp Thr Phe Thr Lys Asn Thr Asn Ser His His Leu Asn 930 935 940 Ser Asn Asn Asn Leu Ser Asn Gly Lys Leu Asp lie Lys Glu Tyr Lys 945 950 955 960 Tyr Arg Asp Val Lys Ala Thr Arg Glu Asp lie lie Leu Met Ser Ser 965 970 975 Val Arg Lys Cys Asn Asn Asn lie Ser Leu Glu Tyr Cys Asn Ser Val 980 985 990 Glu Asp Lys lie Ser Ser Asn Thr Cys Ser Arg Glu Lys Ser Lys Asn 995 1000 1005 Leu Cys Cys Ser lie Ser Asp Phe Cys Leu Asn Tyr Phe Asp Val Tyr 1010 1015 1020 Ser Tyr Glu Tyr Leu Ser Cys Met Lys Lys Glu Phe Glu Asp Pro Ser 1025 1030 1035 1040 Tyr Lys Cys Phe Thr Lys Gly Gly Phe Lys lie Asp Lys Thr Tyr Phe 1045 1050 1055 Ala Ala Ala Gly Ala Leu Leu lie Leu Leu Leu lie Ala Ser Arg Lys 1060 1065 1070 Met lie Lys Asn Asp Ser Glu Glu Ala Thr Phe Asn Glu Phe Glu Glu 1075 1080 1085 Tyr Cys Asp Asn lie His Arg lie Pro Leu Met Pro Asn Asn lie Glu 1090 1095 1100 His Met Gin Pro Ser Thr Pro Leu Asp Tyr Ser 1105 1110 1115 (2) INFORMATION FOR SEQ ID NO:3: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4507 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (iii) HYPOTHETICAL: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Plasmodium falciparum (xi) SEQUENCE DESCRIPTION: SEQ ID NO:3: TATATATATA TATATATATA GATAATAACA TATAAATATA TTCAATGTGC ATACAATGAA 60 ATGTAATATT AGTATATATT TTTTTGCTTC CTTCTTTGTG TTATATTTTG CAAAAGCTAG 120 GAATGAATAT GATATAAAAG AGAATGAAAA ATTTTTAGAC GTGTATAAAG AAAAATTTAA 180 TGAATTAGAT AAAAAGAAAT ATGGAAATGT TCAAAAAACT GATAAGAAAA TATTTACTTT 240 TATAGAAAAT AAATTAGATA TTTTAAATAA TTCAAAATTT AATAAAAGAT GGAAGAGTTA 300 TGGAACTCCA GATAATATAG ATAAAAATAT GTCTTTAATA AATAAACATA ATAATGAAGA 360 AATGTTTAAC AACAATTATC AATCATTTTT ATCGACAAGT TCATTAATAA AGCAAAATAA 420 ATATGTTCCT ATTAACGCTG TACGTGTGTC TAGGATATTA AGTTTCCTGG ATTCTAGAAT 480 TAATAATGGA AGAAATACTT CATCTAATAA CGAAGTTTTA AGTAATTGTA GGGAAAAAAG 540 GAAAGGAATG AAATGGGATT GTAAAAAGAA AAATGATAGA AGCAACTATG TATGTATTCC 600 TGATCGTAGA ATCCAATTAT GCATTGTTAA TCTTAGCATT ATTAAAACAT ATACAAAAGA 660 GACCATGAAG GATCATTTCA TTGAAGCCTC TAAAAAAGAA TCTCAACTTT TGCTTAAAAA 720 AAATGATAAC AAATATAATT CTAAATTTTG TAATGATTTG AAGAATAGTT TTTTAGATTA 780 TGGACATCTT GCTATGGGAA ATGATATGGA TTTTGGAGGT TATTCAACTA AGGCAGAAAA 840 CAAAATTCAA GAAGTTTTTA AAGGGGCTCA TGGGGAAATA AGTGAACATA AAATTAAAAA 900 TTTTAGAAAA GAATGGTGGA ATGAATTTAG AGAGAAACTT TGGGAAGCTA TGTTATCTGA 960 GCATAAAAAT AATATAAATA ATTGTAAAAA TATTCCCCAA GAAGAATTAC AAATTACTCA 1020 ATGGATAAAA GAATGGCATG GAGAATTTTT GCTTGAAAGA GATAATAGAT CAAAATTGCC 1080 AAAAAGTAAA TGTAAAAATA ATACATTATA TGAAGCATGT GAGAAGGAAT GTATTGATCC 1140 ATGTATGAAA TATAGAGATT GGATTATTAG AAGTAAATTT GAATGGCATA CGTTATCGAA 1200 AGAATATGAA ACTCAAAAAG TTCCAAAGGA AAATGCGGAA AATTATTTAA TCAAAATTTC 1260 AGAAAACAAG AATGATGCTA AAGTAAGTTT ATTATTGAAT AATTGTGATG CTGAATATTC 1320 AAAATATTGT GATTGTAAAC ATACTACTAC TCTCGTTAAA AGCGTTTTAA ATGGTAACGA 1380 CAATACAATT AAGGAAAAGC GTGAACATAT TGATTTAGAT GATTTTTCTA AATTTGGATG 1440 TGATAAAAAT TCCGTTGATA CAAACACAAA GGTGTGGGAA TGTAAAAACC CTTATATATT 1500 ATCCACTAAA GATGTATGTG TACCTCCGAG GAGGCAAGAA TTATGTCTTG GAAACATTGA 1560 TAGAATATAC GATAAAAACC TATTAATGAT AAAAGAGCAT ATTCTTGCTA TTGCAATATA 1620 TGAATCAAGA ATATTGAAAC GAAAATATAA GAATAAAGAT GATAAAGAAG TTTGTAAAAT 1680 CATAAATAAA ACTTTCGCTG ATATAAGAGA TATTATAGGA GGTACTGATT ATTGGAATGA 1740 TTTGAGCAAT AGAAAATTAG TAGGAAAAAT TAACACAAAT TCAAAATATG TTCACAGGAA 1800 TAAAAAAAAT GATAAGCTTT TTCGTGATGA GTGGTGGAAA GTTATTAAAA AAGATGTATG 1860 GAATGTGATA TCATGGGTAT TCAAGGATAA AACTGTTTGT AAAGAAGATG ATATTGAAAA 1920 TATACCACAA TTCTTCAGAT GGTTTAGTGA ATGGGGTGAT GATTATTGCC AGGATAAAAC 1980 AAAAATGATA GAGACTCTGA AGGTTGAATG CAAAGAAAAA CCTTGTGAAG ATGACAATTG 2040 TAAAAGTAAA TGTAATTCAT ATAAAGAATG GATATCAAAA AAAAAAGAAG AGTATAATAA 2100 ACAAGCCAAA CAATACCAAG AATATCAAAA AGGAAATAAT TACAAAATGT ATTCTGAATT 2160 TAAATCTATA AAACCAGAAG TTTATTTAAA GAAATACTCG GAAAAATGTT CTAACCTAAA 2220 TTTCGAAGAT GAATTTAAGG AAGAATTACA TTCAGATTAT AAAAATAAAT GTACGATGTG 2280 TCCAGAAGTA AAGGATGTAC CAATTTCTAT AATAAGAAAT AATGAACAAA CTTCGCAAGA 2340 AGCAGTTCCT GAGGAAAACA CTGAAATAGC ACACAGAACG GAAACTCCAT CTATCTCTGA 2400 AGGACCAAAA GGAAATGAAC AAAAAGAACG TGATGACGAT AGTTTGAGTA AAATAAGTGT 2460 ATCACCAGAA AATTCAAGAC CTGAAACTGA TGCTAAAGAT ACTTCTAACT TGTTAAAATT 2520 AAAAGGAGAT GTTGATATTA GTATGCCTAA AGCAGTTATT GGGAGCAGTC CTAATGATAA 2580 TATAAATGTT ACTGAACAAG GGGATAATAT TTCCGGGGTG AATTCTAAAC CTTTATCTGA 2640 TGATGTACGT CCAGATAAAA AGGAATTAGA AGATCAAAAT AGTGATGAAT CGGAAGAAAC 2700 TGTAGTAAAT CATATATCAA AAAGTCCATC TATAAATAAT GGAGATGATT CAGGCAGTGG 2760 AAGTGCAACA GTGAGTGAAT CTAGTAGTTC AAATACTGGA TTGTCTATTG ATGATGATAG 2820 AAATGGTGAT ACATTTGTTC GAACACAAGA TACAGCAAAT ACTGAAGATG TTATTAGAAA 2880 AGAAAATGCT GACAAGGATG AAGATGAAAA AGGCGCAGAT GAAGAAAGAC ATAGTACTTC 2940 TGAAAGCTTA AGTTCACCTG AAGAAAAAAT GTTAACTGAT AATGAAGGAG GAAATAGTTT 3000 AAATCATGAA GAGGTGAAAG AACATACTAG TAATTCTGAT AATGTTCAAC AGTCTGGAGG 3060 AATTGTTAAT ATGAATGTTG AGAAAGAACT AAAAGATACT TTAGAAAATC CTTCTAGTAG 3120 CTTGGATGAA GGAAAAGCAC ATGAAGAATT ATCAGAACCA AATCTAAGCA GTGACCAAGA 3180 TATGTCTAAT ACACCTGGAC CTTTGGATAA CACCAGTGAA GAAACTACAG AAAGAATTAG 3240 TAATAATGAA TATAAAGTTA ACGAGAGGGA AGATGAGAGA ACGCTTACTA AGGAATATGA 3300 AGATATTGTT TTGAAAAGTC ATATGAATAG AGAATCAGAC GATGGTGAAT TATATGACGA 3360 AAATTCAGAC TTATCTACTG TAAATGATGA ATCAGAAGAC GCTGAAGCAA AAATGAAAGG 3420 AAATGATACA TCTGAAATGT CGCATAATAG TAGTCAACAT ATTGAGAGTG ATCAACAGAA 3480 AAACGATATG AAAACTGTTG GTGATTTGGG AACCACACAT GTACAAAACG AAATTAGTGT 3540 TCCTGTTACA GGAGAAATTG ATGAAAAATT AAGGGAAAGT AAAGAATCAA AAATTCATAA 3600 GGCTGAAGAG GAAAGATTAA GTCATACAGA TATACATAAA ATTAATCCTG AAGATAGAAA 3660 TAGTAATACA TTACATTTAA AAGATATAAG AAATGAGGAA AACGAAAGAC ACTTAACTAA 3720 TCAAAACATT AATATTAGTC AAGAAAGGGA TTTGCAAAAA CATGGATTCC ATACCATGAA 3780 TAATCTACAT GGAGATGGAG TTTCCGAAAG AAGTCAAATT AATCATAGTC ATCATGGAAA 3840 CAGACAAGAT CGGGGGGGAA ATTCTGGGAA TGTTTTAAAT ATGAGATCTA ATAATAATAA 3900 TTTTAATAAT ATTCCAAGTA GATATAATTT ATATGATAAA AAATTAGATT TAGATCTTTA 3960 TGAAAACAGA AATGATAGTA CAACAAAAGA ATTAATAAAG AAATTAGCAG AAATAAATAA 4020 ATGTGAGAAC GAAATTTCTG TAAAATATTG TGACCATATG ATTCATGAAG AAATCCCATT 4080 AAAAACATGC ACTAAAGAAA AAACAAGAAA TCTGTGTTGT GCAGTATCAG ATTACTGTAT 4140 GAGCTATTTT ACATATGATT CAGAGGAATA TTATAATTGT ACGAAAAGGG AATTTGATGA 4200 TCCATCTTAT ACATGTTTCA GAAAGGAGGC TTTTTCAAGT ATGATATTCA AATTTTTAAT 4260 AACAAATAAA ATATATTATT ATTTTTATAC TTACAAAACT GCAAAAGTAA CAATAAAAAA 4320 AATTAATTTC TCATTAATTT TTTTTTTCTT TTTTTCTTTT TAGGTATGCC ATATTATGCA 4380 GGAGCAGGTG TGTTATTTAT TATATTGGTT ATTTTAGGTG CTTCACAAGC CAAATATCAA 4440 AGGTTAGAAA AAATAAATAA AAATAAAATT GAGAAGAATG TAAATTAAAT ATAGAATTCG 4500 AGCTCGG 4507 (2) INFORMATION FOR SEQ ID NO:4: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1426 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Plasmodium falciparum (xi) SEQUENCE DESCRIPTION: SEQ ID NO:4: Met Lys Cys Asn lie Ser lie Tyr Phe Phe Ala Ser Phe Phe Val Leu 1 5 10 15 Tyr Phe Ala Lys Ala Arg Asn Glu Tyr Asp lie Lys Glu Asn Glu Lys 20 25 30 Phe Leu Asp Val Tyr Lys Glu Lys Phe Asn Glu Leu Asp Lys Lys Lys 35 40 45 Tyr Gly Asn Val Gin Lys Thr Asp Lys Lys lie Phe Thr Phe lie Glu 50 55 60 Asn Lys Leu Asp lie Leu Asn Asn Ser Lys Phe Asn Lys Arg Trp Lys 65 70 75 80 Ser Tyr Gly Thr Pro Asp Asn lie Asp Lys Asn Met Ser Leu lie Asn 85 90 95 Lys His Asn Asn Glu Glu Met Phe Asn Asn Asn Tyr Gin Ser Phe Leu 100 105 110 Ser Thr Ser Ser Leu lie Lys Gin Asn Lys Tyr Val Pro lie Asn Ala 115 120 125 Val Arg Val Ser Arg lie Leu Ser Phe Leu Asp Ser Arg lie Asn Asn 130 135 140 Gly Arg Asn Thr Ser Ser Asn Asn Glu Val Leu Ser Asn Cys Arg Glu 145 150 155 160 Lys Arg Lys Gly Met Lys Trp Asp Cys Lys Lys Lys Asn Asp Arg Ser 165 170 175 Asn Tyr Val Cys lie Pro Asp Arg Arg lie Gin Leu Cys lie Val Asn 180 185 190 Leu Ser lie lie Lys Thr Tyr Thr Lys Glu Thr Met Lys Asp His Phe 195 200 205 lie Glu Ala Ser Lys Lys Glu Ser Gin Leu Phe Ser Leu Lys Asn Asp 210 215 220 Asn Lys Tyr Asn Ser Lys Phe Cys Asn Asp Leu Lys Asn Ser Phe Leu 225 230 235 240 Asp Tyr Gly His Leu Ala Met Gly Asn Asp Met Asp Phe Gly Gly Tyr 245 250 255 Ser Thr Lys Ala Glu Asn Lys He Gin Glu Val Phe Lys Gly Ala His 260 265 270 Gly Glu He Ser Glu His Lys He Lys Asn Phe Arg Lys Glu Trp Trp 275 280 285 Asn Glu Phe Arg Glu Lys Leu Trp Glu Ala Met Leu Ser Glu His Lys 290 295 300 Asn Asn He Asn Asn Cys Lys Asn He Ser Gin Glu Glu Leu Gin He 305 310 315 320 Thr Gin Trp He Lys Glu Trp His Gly Glu Phe Leu Leu Glu Arg Asp 325 330 335 Asn Arg Ser Lys Leu Pro Lys Ser Lys Cys Lys Asn Asn Thr Leu Tyr 340 345 350 Glu Ala Cys Glu Lys Glu Cys He Asp Pro Cys Met Lys Tyr Arg Asp 355 360 365 Trp He He Arg Ser Lys Phe Glu Trp His Thr Leu Ser Lys Glu Tyr 370 375 380 Glu Thr Gin Lys Val Pro Lys Glu Asn Ala Glu Asn Tyr Leu He Lys 385 390 395 400 He Ser Glu Asn Lys Asn Asp Ala Lys Val Ser Leu Leu Leu Asn Asn 405 410 415 Cys Asp Ala Glu Tyr Ser Lys Tyr Cys Asp Cys Lys His Thr Thr Thr 420 425 430 Leu Val Lys Ser Val Leu Asn Gly Asn Asp Asn Thr He Lys Glu Lys 435 440 445 Arg Glu His He Asp Leu Asp Asp Phe Ser Lys Phe Gly Cys Asp Lys 450 455 460 Asn Ser Val Asp Thr Asn Thr Lys Val Trp Glu Cys Lys Asn Pro Tyr 465 470 475 480 He Leu Ser Thr Lys Asp Val Cys Val Pro Pro Arg Arg Gin Glu Leu 485 490 495 Cys Leu Gly Asn He Asp Arg He Tyr Asp Lys Asn Leu Leu Met He 500 505 510 Lys Glu His He Leu Ala He Ala He Tyr Glu Ser Arg He Leu Lys 515 520 525 Arg Lys Tyr Lys Asn Lys Asp Asp Lys Glu Val Cys Lys He He Asn 530 535 540 Lys Thr Phe Ala Asp He Arg Asp He He Gly Gly Thr Asp Tyr Trp 545 550 555 560 Asn Asp Leu Ser Asn Arg Lys Leu Val Gly Lys He Asn Thr Asn Ser 565 570 575 Lys Tyr Val His Arg Asn Lys Lys Asn Asp Lys Leu Phe Arg Asp Glu 580 585 590 Trp Trp Lys Val He Lys Lys Asp Val Trp Asn Val He Ser Trp Val 595 600 605 Phe Lys Asp Lys Thr Val Cys Lys Glu Asp Asp He Glu Asn He Pro 610 615 620 Gin Phe Phe Arg Trp Phe Ser Glu Trp Gly Asp Asp Tyr Cys Gin Asp 625 630 635 640 Lys Thr Lys Met He Glu Thr Leu Lys Val Glu Cys Lys Glu Lys Pro 645 650 655 Cys Glu Asp Asp Asn Cys Lys Ser Lys Cys Asn Ser Tyr Lys Glu Trp 660 665 670 He Ser Lys Lys Lys Lys Ser He He Thr Ser Asn He Pro Arg He 675 680 685 Ser Lys Arg Asn Asn Tyr Lys Met Tyr Ser Glu Phe Lys Ser He Lys 690 695 700 Pro Glu Val Tyr Leu Lys Lys Tyr Ser Lys Cys Ser Asn Leu Asn Phe 705 710 715 720 Glu Asp Glu Phe Lys Glu Glu Leu His Ser Asp Tyr Lys Asn Lys Cys 725 730 735 Thr Met Cys Pro Glu Val Lys Asp Val Pro He Ser He He Arg Asn 740 745 750 Asn Glu Gin Thr Ser Gin Glu Ala Val Pro Glu Glu Asn Thr Glu He 755 760 765 Ala His Arg Thr Glu Thr Pro Ser He Ser Glu Gly Pro Lys Gly Asn 770 775 780 Glu Gin Lys Glu Arg Asp Asp Asp Ser Leu Ser Lys He Ser Val Ser 785 790 795 800 Pro Glu Asn Ser Arg Pro Glu Thr Asp Ala Lys Asp Thr Ser Asn Leu 805 810 815 Leu Lys Leu Lys Gly Asp Val Asp He Ser Met Pro Lys Ala Val He 820 825 830 Gly Ser Ser Pro Asn Asp Asn He Asn Val Thr Glu Gin Gly Asp Asn 835 840 845 He Ser Gly Val Asn Ser Lys Pro Leu Ser Asp Asp Val Arg Pro Asp 850 855 860 Lys Lys Glu Leu Glu Asp Gin Asn Ser Asp Glu Ser Glu Glu Thr Val 865 870 875 880 Val Asn His He Ser Lys Ser Pro Ser He Asn Asn Gly Asp Asp Ser 885 890 895 Gly Ser Gly Ser Ala Thr Val Ser Glu Ser Ser Ser Ser Asn Thr Gly 900 905 910 Leu Ser He Asp Asp Asp Arg Asn Gly Asp Thr Phe Val Arg Thr Gin 915 920 925 Asp Thr Ala Asn Thr Glu Asp Val He Arg Lys Glu Asn Ala Asp Lys 930 935 940 Asp Glu Asp Glu Lys Gly Ala Asp Glu Glu Arg His Ser Thr Ser Glu 945 950 955 960 Ser Leu Ser Ser Pro Glu Glu Lys Met Leu Thr Asp Asn Glu Gly Gly 965 970 975 Asn Ser Leu Asn His Glu Glu Val Lys Glu His Thr Ser Asn Ser Asp 980 985 990 Asn Val Gin Gin Ser Gly Gly He Val Asn Met Asn Val Glu Lys Glu 995 1000 1005 Leu Lys Asp Thr Leu Glu Asn Pro Ser Ser Ser Leu Asp Glu Gly Lys 1010 1015 1020 Ala His Glu Glu Leu Ser Glu Pro Asn Leu Ser Ser Asp Gin Asp Met 1025 1030 1035 1040 Ser Asn Thr Pro Gly Pro Leu Asp Asn Thr Ser Glu Glu Thr Thr Glu 1045 1050 1055 Arg He Ser Asn Asn Glu Tyr Lys Val Asn Glu Arg Glu Asp Glu Arg 1060 1065 1070 Thr Leu Thr Lys Glu Tyr Glu Asp He Val Leu Lys Ser His Met Asn 1075 1080 1085 Arg Glu Ser Asp Asp Gly Glu Leu Tyr Asp Glu Asn Ser Asp Leu Ser 1090 1095 1100 Thr Val Asn Asp Glu Ser Glu Asp Ala Glu Ala Lys Met Lys Gly Asn 1105 1110 1115 1120 Asp Thr Ser Glu Met Ser His Asn Ser Ser Gin His He Glu Ser Asp 1125 1130 1135 Gin Gin Lys Asn Asp Met Lys Thr Val Gly Asp Leu Gly Thr Thr His 1140 1145 1150 Val Gin Asn Glu He Ser Val Pro Val Thr Gly Glu He Asp Glu Lys 1155 1160 1165 Leu Arg Glu Ser Lys Glu Ser Lys He His Lys Ala Glu Glu Glu Arg 1170 1175 1180 Leu Ser His Thr Asp He His Lys He Asn Pro Glu Asp Arg Asn Ser 1185 1190 1195 1200 Asn Thr Leu His Leu Lys Asp He Arg Asn Glu Glu Asn Glu Arg His 1205 1210 1215 Leu Thr Asn Gin Asn He Asn He Ser Gin Glu Arg Asp Leu Gin Lys 1220 1225 1230 Ala Val Asp Ser Met Glu Met Glu Phe Pro Lys Glu Val Lys Leu He 1235 1240 1245 He Val He Met Glu Thr Asp Lys He Gly Gly Asn Ser Gly Asn Val 1250 1255 1260 Leu Asn Met Arg Ser Asn Asn Asn Asn Phe Asn Asn He Pro Ser Arg 1265 1270 1275 1280 Tyr Asn Leu Tyr Asp Lys Lys Leu Asp Leu Asp Leu Tyr Glu Asn Arg 1285 1290 1295 Asn Asp Ser Thr Thr Lys Glu Leu He Lys Lys Leu Ala Glu He Asn 1300 1305 1310 Lys Cys Glu Asn Glu He Ser Val Lys Tyr Cys Asp His Met He His 1315 1320 1325 Glu Glu He Pro Leu Lys Thr Cys Thr Lys Glu Lys Thr Arg Asn Leu 1330 1335 1340 Cys Cys Ala Val Ser Asp Tyr Cys Met Ser Tyr Phe Thr Tyr Asp Ser 1345 1350 1355 1360 Glu Glu Tyr Tyr Asn Cys Thr Lys Arg Glu Phe Asp Asp Pro Ser Tyr 1365 1370 1375 Thr Cys Phe Arg Lys Glu Ala Phe Ser Ser Met He Phe Lys Phe Leu 1380 1385 1390 He Thr Asn Lys He Tyr Tyr Tyr Phe Tyr Thr Tyr Lys Thr Ala Lys 1395 1400 1405 Val Thr He Lys Lys He Asn Phe Ser Leu He Phe Phe Phe Phe Phe 1410 1415 1420 Ser Phe 1425 (2) INFORMATION FOR SEQ ID NO:5: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2288 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (iii) HYPOTHETICAL: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Plasmodium falciparum (xi) SEQUENCE DESCRIPTION: SEQ ID NO:5: CACTTTATGC TTCCGGCTCG TATGTTGTGT GGAATTGTGA GCGGATAACA ATTTCACACA 60 GGAAACAGCT ATGACCATGA TTACGCCAAG CTCTAATACG ACTCACTATA GGGAAAGCTG 120 GTACGCCTGC AGGTCCGGTC CGGAATTCAA TAAAATATTT CCAGAAAGGA ATGTGCAAAT 180 TCACATATCC AATATATTCA AGGAATATAA AGAAAATAAT GTAGATATCA TATTTGGAAC 240 GTTGAATTAT GAATATAATA ATTTCTGTAA AGAAAAACCT GAATTAGTAT CTGCTGCCAA 300 GTATAATCTG AAAGCTCCAA ATGCTAAATC CCCTAGAATA TACAAATCTA AGGAGCATGA 360 AGAATCAAGT GTGTTTGGTT GCAAAACGAA AATCAGTAAA GTTAAAAAAA AATGGAATTG 420 TTATAGTAAT AATAAAGTAA CTAAACCTGA AGGTGTATGT GGACCACCAA GAAGGCAACA 480 ATTATGTCTT GGATATATAT TTTTGATTCG CGACGGTAAC GAGGAAGGAT TAAAAGATCA 540 TATTAATAAG GCAGCTAATT ATGAGGCAAT GCATTTAAAA GAGAAATATG AGAATGCTGG 600 TGGTGATAAA ATTTGCAATG CTATATTGGG AAGTTATGCA GATATTGGAG ATATTGTAAG 660 AGGTTTGGAT GTTTGGAGGG ATATAAATAC TAATAAATTA TCAGAAAAAT TCCAAAAAAT 720 TTTTATGGGT GGTGGTAATT CTAGGAAAAA ACAAAACGAT AATAATGAAC GTAATAAATG 780 GTGGGAAAAA CAAAGGAATT TAATATGGTC TAGTATGGTA AAACACATTC CAAAAGGAAA 840 AACATGTAAA CGTCATAATA ATTTTGAGAA AATTCCTCAA TTTTTGAGAT GGTTAAAAGA 900 ATGGGGTGAT GAATTTTGTG AGGAAATGGG TACGGAAGTC AAGCAATTAG AGAAAATATG 960 TGAAAATAAA AATTGTTCGG AAAAAAAATG TAAAAATGCA TGTAGTTCCT ATGAAAAATG 1020 GATAAAGGAA CGAAAAAATG AATATAATTT GCAATCAAAG AAATTTGATA GTGATAAAAA 1080 ATTAAATAAA AAAAACAATC TTTATAATAA ATTTGAGGAT TCTAAAGCTT ATTTAAGGAG 1140 TGAATCAAAA CAGTGCTCAA ATATAGAATT TAATGATGAA ACATTTACAT TTCCTAATAA 1200 ATATAAAGAG GCTTGTATGG TATGTGAAAA TCCTTCATCT TCGAAAGCTC TTAAACCTAT 1260 AAAAACGAAT GTGTTTCCTA TAGAGGAATC AAAAAAATCT GAGTTATCAA GTTTAACAGA 1320 TAAATCTAAG AATACTCCTA ATAGTTCTGG TGGGGGAAAT TATGGAGATA GACAAATATC 1380 AAAAAGAGAC GATGTTCATC ATGATGGTCC TAAGGAAGTG AAATCCGGAG AAAAAGAGGT 1440 ACCAAAAATA GATGCAGCTG TTAAAACAGA AAATGAATTT ACCTCTAATC GAAACGATAT 1500 TGAAGGAAAG GAAAAAAGTA AAGGTGATCA TTCTTCTCCT GTTCATTCTA AAGATATAAA 1560 AAATGAGGAA CCACAAAGGG TGGTGTCTGA AAATTTACCT AAAATTGAAG AGAAAATGGA 1620 ATCTTCTGAT TCTATACCAA TTACTCATAT AGAAGCTGAA AAGGGTCAGT CTTCTAATTC 1680 TAGCGATAAT GATCCTGCAG TAGTAAGTGG TAGAGAATCT AAAGATGTAA ATCTTCATAC 1740 TTCTGAAAGG ATTAAAGAAA ATGAAGAAGG TGTGATTAAA ACAGATGATA GTTCAAAAAG 1800 TATTGAAATT TCTAAAATAC CATCTGACCA AAATAATCAT AGTGATTTAT CACAGAATGC 1860 AAATGAGGAC TCTAATCAAG GGAATAAGGA AACAATAAAT CCTCCTTCTA CAGAAAAAAA 1920 TCTCAAAGAA ATTCATTATA AAACATCTGA TTCTGATGAT CATGGTTCTA AAATTAAAAG 1980 TGAAATTGAA CCAAAGGAGT TAACGGAGGA ATCACCTCTT ACTGATAAAA AAACTGAAAG 2040 TGCAGCGATT GGTGATAAAA ATCATGAATC AGTAAAAAGC GCTGATATTT TTCAATCTGA 2100 GATTCATAAT TCTGATAATA GAGATAGAAT TGTTTCTGAA AGTGTAGTTC AGGATTCTTC 2160 AGGAAGCTCT ATGAGTACTG AATCTATACG TACTGATAAC AAGGATTTTA AAACAAGTGA 2220 GGATATTGCA CCTTCTATTA ATGGTCGGAA TTCCCGGGTC GACGAGCTCA CTAGTCGGCG 2280 GCCGCTCT 2288 (2) INFORMATION FOR SEQ ID NO:6: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 749 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Plasmodium falciparum (xi) SEQUENCE DESCRIPTION: SEQ ID NO:6: Ala Asp Asn Asn Phe Thr Gin Glu Thr Ala Met Thr Met He Thr Pro 1 5 10 15 Ser Ser Asn Thr Thr His Tyr Arg Glu Ser Trp Tyr Ala Cys Arg Ser 20 25 30 Gly Pro Glu Phe Asn Lys He Phe Pro Glu Arg Asn Val Gin He His 35 40 45 He Ser Asn He Phe Lys Glu Tyr Lys Glu Asn Asn Val Asp He He 50 55 60 Phe Gly Thr Leu Asn Tyr Glu Tyr Asn Asn Phe Cys Lys Glu Lys Pro 65 70 75 80 Glu Leu Val Ser Ala Ala Lys Tyr Asn Leu Lys Ala Pro Asn Ala Lys 85 90 95 Ser Pro Arg He Tyr Lys Ser Lys Glu His Glu Glu Ser Ser Val Phe 100 105 110 Gly Cys Lys Thr Lys He Ser Lys Val Lys Lys Lys Trp Asn Cys Tyr 115 120 125 Ser Asn Asn Lys Val Thr Lys Pro Glu Gly Val Cys Gly Pro Pro Arg 130 135 140 Arg Gin Gin Leu Cys Leu Gly Tyr He Phe Leu He Arg Asp Gly Asn 145 150 155 160 Glu Glu Gly Leu Lys Asp His He Asn Lys Ala Ala Asn Tyr Glu Ala 165 170 175 Met His Leu Lys Glu Lys Tyr Glu Asn Ala Gly Gly Asp Lys He Cys 180 185 190 Asn Ala He Leu Gly Ser Tyr Ala Asp He Gly Asp He Val Arg Gly 195 200 205 Leu Asp Val Trp Arg Asp He Asn Thr Asn Lys Leu Ser Glu Lys Phe 210 215 220 Gin Lys He Phe Met Gly Gly Gly Asn Ser Arg Lys Lys Gin Asn Asp 225 230 235 240 Asn Asn Glu Arg Asn Lys Trp Trp Glu Lys Gin Arg Asn Leu He Trp 245 250 255 Ser Ser Met Val Lys His He Pro Lys Gly Lys Thr Cys Lys Arg His 260 265 270 Asn Asn Phe Glu Lys He Pro Gin Phe Leu Arg Trp Leu Lys Glu Trp 275 280 285 Gly Asp Glu Phe Cys Glu Glu Met Gly Thr Glu Val Lys Gin Leu Glu 290 295 300 Lys He Cys Glu Asn Lys Asn Cys Ser Glu Lys Lys Cys Lys Asn Ala 305 310 315 320 Cys Ser Ser Tyr Glu Lys Trp He Lys Glu Arg Lys Asn Glu Tyr Asn 325 330 335 Leu Gin Ser Lys Lys Phe Asp Ser Asp Lys Lys Leu Asn Lys Lys Asn 340 345 350 Asn Leu Tyr Asn Lys Phe Glu Asp Ser Lys Ala Tyr Leu Arg Ser Glu 355 360 365 Ser Lys Gin Cys Ser Asn He Glu Phe Asn Asp Glu Thr Phe Thr Phe 370 375 380 Pro Asn Lys Tyr Lys Glu Ala Cys Met Val Cys Glu Asn Pro Ser Ser 385 390 395 400 Ser Lys Ala Leu Lys Pro He Lys Thr Asn Val Phe Pro He Glu Glu 405 410 415 Ser Lys Lys Ser Glu Leu Ser Ser Leu Thr Asp Lys Ser Lys Asn Thr 420 425 430 Pro Asn Ser Ser Gly Gly Gly Asn Tyr Gly Asp Arg Gin He Ser Lys 435 440 445 Arg Asp Asp Val His His Asp Gly Pro Lys Glu Val Lys Ser Gly Glu 450 455 460 Lys Glu Val Pro Lys He Asp Ala Ala Val Lys Thr Glu Asn Glu Phe 465 470 475 480 Thr Ser Asn Arg Asn Asp He Glu Gly Lys Glu Lys Ser Lys Gly Asp 485 490 495 His Ser Ser Pro Val His Ser Lys Asp He Lys Asn Glu Glu Pro Gin 500 505 510 Arg Val Val Ser Glu Asn Leu Pro Lys He Glu Glu Lys Met Glu Ser 515 520 525 Ser Asp Ser He Pro He Thr His He Glu Ala Glu Lys Gly Gin Ser 530 535 540 Ser Asn Ser Ser Asp Asn Asp Pro Ala Val Val Ser Gly Arg Glu Ser 545 550 555 560 Lys Asp Val Asn Leu His Thr Ser Glu Arg He Lys Glu Asn Glu Glu 565 570 575 Gly Val He Lys Thr Asp Asp Ser Ser Lys Ser He Glu He Ser Lys 580 585 590 He Pro Ser Asp Gin Asn Asn His Ser Asp Leu Ser Gin Asn Ala Asn 595 600 605 Glu Asp Ser Asn Gin Gly Asn Lys Glu Thr He Asn Pro Pro Ser Thr 610 615 620 Glu Lys Asn Leu Lys Glu He His Tyr Lys Thr Ser Asp Ser Asp Asp 625 630 635 640 His Gly Ser Lys He Lys Ser Glu He Glu Pro Lys Glu Leu Thr Glu 645 650 655 Glu Ser Pro Leu Thr Asp Lys Lys Thr Glu Ser Ala Ala He Gly Asp 660 665 670 Lys Asn His Glu Ser Val Lys Ser Ala Asp He Phe Gin Ser Glu He 675 680 685 His Asn Ser Asp Asn Arg Asp Arg He Val Ser Glu Ser Val Val Gin 690 695 700 Asp Ser Ser Gly Ser Ser Met Ser Thr Glu Ser He Arg Thr Asp Asn 705 710 715 720 Lys Asp Phe Lys Thr Ser Glu Asp He Ala Pro Ser He Asn Gly Arg 725 730 735 Asn Ser Arg Val Asp Glu Leu Thr' Ser Arg Arg Pro Leu 740 745 (2) INFORMATION FOR SEQ ID NO:7: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2606 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (iii) HYPOTHETICAL: NO (Vi) ORIGINAL SOURCE: (A) ORGANISM: Plasmodium falciparum ( i) SEQUENCE DESCRIPTION: SEQ ID NO:7: AGCTCTATTA CGACTCACTA TAGGGAAAGC TGGTACGCCT GCAGGTACCG GTCCGGAATT 60 CCCGGGTCGA CGAGCTCACT AGTCGGCGGC CGCTCTAGAG GATCCAAGCT TAATAGTGTT 120 TATACGTCTA TTGGCTTATT TTTAAATAGC TTAAAAAGCG GACCATGTAA AAAGGATAAT 180 GATAATGCAG AGGATAATAT AGATTTTGGT GATGAAGGTA AAACATTTAA AGAGGCAGAT 240 AATTGTAAAC CATGTTCTCA ATTTACTGTT GATTGTAAAA ATTGTAATGG TGGTGATACA 300 AAAGGGAAGT GCAATGGCAG CAATGGCAAA AAGAATGGAA ATGATTATAT TACTGCAAGT 360 GATATTGAAA ATGGAGGGAA TTCTATTGGA AATATAGATA TGGTTGTTAG TGATAAGGAT 420 GCAAATGGAT TTAATGGTTT AGACGCTTGT GGAAGTGCAA ATATCTTTAA AGGTATTAGA 480 AAAGAACAAT GGAAATGTGC TAAAGTATGT GGTTTAGATG TATGTGGTCT TAAAAATGGT 540 AATGGTAGTA TAGATAAAGA TCAAAAACAA ATTATAATTA TTAGAGCATT GCTTAAACGT 600 TGGGTAGAAT ATTTTTTAGA AGATTATAAT AAAATTAATG CCAAAATTTC ACATTGTACG 660 AAAAAGGATA ATGAATCCAC ATGTACAAAT GATTGTCCAA ATAAATGTAC ATGTGTAGAA 720 GAGTGGATAA ATCAGAAAAG GACAGAATGG AAAAATATAA AAAAACATTA CAAAACACAA 780 AATGAAAATG GTGACAATAA CATGAAATCT TTGGTTACAG ATATTTTGGG TGCCTTGCAA 840 CCCCAAAGTG ATGTTAACAA AGCTATAAAA CCTTGTAGTG GTTTAACTGC GTTCGAGAGT 900 TTTTGTGGTC TTAATGGCGC TGATAACTCA GAAAAAAAAG AAGGTGAAGA TTACGATCTT 960 GTTCTATGTA TGCTTAAAAA TCTTGAAAAA CAAATTCAGG AGTGCAAAAA GAAACATGGC 1020 GAAACTAGTG TCGAAAATGG TGGCAAATCA TGTACCCCCC TTGACAACAC CACCCTTGAG 1080 GAGGAACCCA TAGAAGAGGA AAACCAAGTG GAAGCGCCGA ACATTTGTCC AAAACAAACA 1140 GTGGAAGATA AAAAAAAAGA GGAAGAAGAA GAAACTTGTA CACCGGCATC ACCAGTACCA 1200 GAAAAACCGG TACCTCATGT GGCACGTTGG CGAACATTTA CACCACCTGA GGTATTCAAG 1260 ATATGGAGGG GAAGGAGAAA TAAAACTACG TGCGAAATAG TGGCAGAAAT GCTTAAAGAT 1320 AAGAATGGAA GGACTACAGT AGGTGAATGT TATAGAAAAG AAACTTATTC TGAATGGACG 1380 TGTGATGAAA GTAAGATTAA AATGGGACAG CATGGAGCAT GTATTCCTCC AAGAAGACAA 1440 AAATTATGTT TACATTATTT AGAAAAAATA ATGACAAATA CAAATGAATT GAAATACGCA 1500 TTTATTAAAT GTGCTGCAGC AGAAACTTTT TTGTTATGGC AAAACTACAA AAAAGATAAG 1560 AATGGTAATG CAGAAGATCT CGATGAAAAA TTAAAAGGTG GTATTATCCC CGAAGATTTT 1620 AAACGGCAAA TGTTCTATAC GTTTGCAGAT TATAGAGATA TATGTTTGGG TACGGATATA 1680 TCATCAAAAA AAGATACAAG TAAAGGTGTA GGTAAAGTAA AATGCAATAT TGATGATGTT 1740 TTTTATAAAA TTAGCAATAG TATTCGTTAC CGTAAAAGTT GGTGGGAAAC AAATGGTCCA 1800 GTTATATGGG AAGGAATGTT ATGCGCTTTA AGTTATGATA CGAGCCTAAA TAATGTTAAT 1860 CCGGAAACTC ACAAAAAACT TACCGAAGGC AATAACAACT TTGAGAAAGT CATATTTGGT 1920 AGTGATAGTA GCACTACTTT GTCCAAATTT TCTGAAAGAC CTCAATTTCT AAGATGGTTG 1980 ACTGAATGGG GAGAAAATTT CTGCAAAGAA CAAAAAAAGG AGTATAAGGT GTTGTTGGCA 2040 AAATGTAAGG ATTGTGATGT TGATGGTGAT GGTAAATGTA ATGGAAAATG TGTTGCGTGC 2100 AAAGATCAAT GTAAACAATA TCATAGTTGG ATTGGAATAT GGATAGATAA TTATAAAAAA 2160 CAAAAAGGAA GATATACTGA GGTTAAAAAA ATACCTCTGT ATAAAGAAGA TAAAGACGTG 2220 AAAAACTCAG ATGATGCTCG CGATTATTTA AAAACACAAT TACAAAATAT GAAATGTGTA 2280 AATGGAACTA CTGATGAAAA TTGTGAGTAT AAGTGTATGC ATAAAACCTC ATCCACAAAT 2340 AGTGATATGC CCGAATCGTT GGACGAAAAG CCGGAAAAGG TCAAAGACAA GTGTAATTGT 2400 GTACCTAATG AATGCAATGC ATTGAGTGTA AGTGGTAGCG GTTTTCCTGA TGGTCAAGCT 2460 TACGTACGCG TGCATGCGAC GTCATAGCTC TTCTATAGTG TCACCTAAAT TCAATTCACT 2520 GGCCGTCGTT TTACAACGTC GTGACTGGGA AAACCTGGCG TTACCCAACT TAATCGCCTT 2580 GCAGCACATC CCCCTTTCGC CAGCTG 2606 (2) INFORMATION FOR SEQ ID NO:8: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 921 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Plasmodium falciparum (xi) SEQUENCE DESCRIPTION: SEQ ID NO:8: Lys Leu Asn Ser Val Tyr Thr Ser He Gly Leu Phe Leu Asn Ser Leu 1 5 10 15 Lys Ser Gly Pro Cys Lys Lys Asp Asn Asp Asn Ala Glu Asp Asn He 20 25 30 Asp Phe Gly Asp Glu Gly Lys Thr Phe Lys Glu Ala Asp Asn Cys Lys 35 40 45 Pro Cys Ser Gin Phe Thr Val Asp Cys Lys Asn Cys Asn Gly Gly Asp 50 55 60 Thr Lys Gly Lys Cys Asn Gly Ser Asn Gly Lys Lys Asn Gly Asn Asp 65 70 75 80 Tyr He Thr Ala Ser Asp He Glu Asn Gly Gly Asn Ser He Gly Asn 85 90 95 He Asp Met Val Val Ser Asp Lys Asp Ala Asn Gly Phe Asn Gly Leu 100 105 110 Asp Ala Cys Gly Ser Ala Asn He Phe Lys Gly He Arg Lys Glu Gin 115 120 125 Trp Lys Cys Ala Lys Val Cys Gly Leu Asp Val Cys Gly Leu Lys Asn 130 135 140 Gly Asn Gly Ser He Asp Lys Asp Gin Lys Gin He He He He Arg 145 150 155 160 Ala Leu Leu Lys Arg Trp Val Glu Tyr Phe Leu Glu Asp Tyr Asn Lys 165 170 175 He Asn Ala Lys He Ser His Cys Thr Lys Lys Asp Asn Glu Ser Thr 180 185 190 Cys Thr Asn Asp Cys Pro Asn Lys Cys Thr Cys Val Glu Glu Trp He 195 200 205 Asn Gin Lys Arg Thr Glu Trp Lys Asn He Lys Lys His Tyr Lys Thr 210 215 220 Gin Asn Glu Asn Gly Asp Asn Asn Met Lys Ser Leu Val Thr Asp He 225 230 235 240 Leu Gly Ala Leu Gin Pro Gin Ser Asp Val Asn Lys Ala He Lys Pro 245 250 255 Cys Ser Gly Leu Thr Ala Phe Glu Ser Phe Cys Gly Leu Asn Gly Ala 260 265 270 Asp Asn Ser Glu Lys Lys Glu Gly Glu Asp Tyr Asp Leu Val Leu Cys 275 280 285 Met Leu Lys Asn Leu Glu Lys Gin He Gin Glu Cys Lys Lys Lys His 290 295 300 Gly Glu Thr Ser Val Glu Asn Gly Gly Lys Ser Cys Thr Pro Leu Asp 305 310 315 320 Asn Thr Thr Leu Glu Glu Glu Pro He Glu Glu Glu Asn Gin Val Glu 325 330 335 Ala Pro Asn He Cys Pro Lys Gin Thr Val Glu Asp Lys Lys Lys Glu 340 345 350 Glu Glu Glu Glu Thr Cys Thr Pro Ala Ser Pro Val Pro Glu Lys Pro 355 360 365 Val Pro His Val Ala Arg Trp Arg Thr Phe Thr Pro Pro Glu Val Phe 370 375 380 Lys He Trp Arg Gly Arg Arg Asn Lys Thr Thr Cys Glu He Val Ala 385 390 395 400 Glu Met Leu Lys Asp Lys Asn Gly Arg Thr Thr Val Gly Glu Cys Tyr 405 410 415 Arg Lys Glu Thr Tyr Ser Glu Trp Thr Cys Asp Glu Ser Lys He Lys 420 425 430 Met Gly Gin His Gly Ala Cys He Pro Pro Arg Arg Gin Lys Leu Cys 435 440 445 Leu His Tyr Leu Glu Lys He Met Thr Asn Thr Asn Glu Leu Lys Tyr 450 455 460 Ala Phe He Lys Cys Ala Ala Ala Glu Thr Phe Leu Leu Trp Gin Asn 465 470 475 480 Tyr Lys Lys Asp Lys Asn Gly Asn Ala Glu Asp Leu Asp Glu Lys Leu 485 490 495 Lys Gly Gly He He Pro Glu Asp Phe Lys Arg Gin Met Phe Tyr Thr 500 505 510 Phe Ala Asp Tyr Arg Asp He Cys Leu Gly Thr Asp He Ser Ser Lys 515 520 525 Lys Asp Thr Ser Lys Gly Val Gly Lys Val Lys Cys Asn He Asp Asp 530 535 540 Val Phe Tyr Lys He Ser Asn Ser He Arg Tyr Arg Lys Ser Trp Trp 545 550 555 560 Glu Thr Asn Gly Pro Val He Trp Glu Gly Met Leu Cys Ala Leu Ser 565 570 575 Tyr Asp Thr Ser Leu Asn Asn Val Asn Pro Glu Thr His Lys Lys Leu 580 585 590 Thr Glu Gly Asn Asn Asn Phe Glu Lys Val He Phe Gly Ser Asp Ser 595 600 605 Ser Thr Thr Leu Ser Lys Phe Ser Glu Arg Pro Gin Phe Leu Arg Trp 610 615 620 Leu Thr Glu Trp Gly Glu Asn Phe Cys Lys Glu Gin Lys Lys Glu Tyr 625 630 635 640 Lys Val Leu Leu Ala Lys Cys Lys Asp Cys Asp Val Asp Gly Asp Gly 645 650 655 Lys Cys Asn Gly Lys Cys Val Ala Cys Lys Asp Gin Cys Lys Gin Tyr 660 665 670 His Ser Trp He Gly He Trp He Asp Asn Tyr Lys Lys Gin Lys Gly 675 680 685 Arg Tyr Thr Glu Val Lys Lys He Pro Leu Tyr Lys Glu Asp Lys Asp 690 695 700 Val Lys Asn Ser Asp Asp Ala Arg Asp Tyr Leu Lys Thr Gin Leu Gin 705 710 715 720 Asn Met Lys Cys Val Asn Gly Thr Thr Asp Glu Asn Cys Glu Tyr Lys 725 730 735 Cys Met His Lys Thr Ser Ser Thr Asn Ser Asp Met Pro Glu Ser Leu 740 745 750 Asp Glu Lys Pro Glu Lys Val Lys Asp Lys Cys Asn Cys Val Pro Asn 755 760 765 Glu Cys Asn Ala Leu Ser Val Ser Gly Ser Gly Phe Pro Asp Gly Gin 770 775 780 Ala Phe Gly Gly Gly Val Leu Glu Gly Thr Cys Lys Gly Leu Gly Glu 785 790 795 800 Pro Lys Lys Lys He Glu Pro Pro Gin Tyr Asp Pro Thr Asn Asp He 805 810 815 Leu Lys Ser Thr He Pro Val Thr He Val Leu Ala Leu Gly Ser He 820 825 830 Ala Phe Leu Phe Met Lys Val He Tyr He Tyr Val Trp Tyr He Tyr 835 840 845 Met Leu Cys Val Gly Ala Leu Asp Thr Tyr He Cys Gly Cys He Cys 850 855 860 He Cys He Phe He Cys Val Ser Val Tyr Val Cys Val Tyr Val Tyr 865 870 875 880 Val Phe Leu Tyr Met Cys Val Phe Tyr He Tyr Phe He Tyr He Tyr 885 890 895 Val Phe He Leu Lys Met Lys Lys Met Lys Lys Met Lys Lys Met Lys 900 905 910 Lys Met Lys Lys Arg Lys Lys Arg He 915 920 (2) INFORMATION FOR SEQ ID NO:9: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2101 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (iii) HYPOTHETICAL: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Plasmodium falciparum (xi) SEQUENCE DESCRIPTION: SEQ ID NO:9: GGAACAGGGT GATAATAAAG TAGGAGCCTG TGCTCCGTAT AGACGATTAC ATTTATGTGA 60 TTATAATTTG GAATCTATAG ACACAACGTC GACGACGCAT AAGTTGTTGT TAGAGGTGTG 120 TATGGCAGCA AAATACGAAG GAAACTCAAT AAATACACAT TATACACAAC ATCAACGAAC 180 TAATGAGGAT TCTGCTTCCC AATTATGTAC TGTATTAGCA CGAAGTTTTG CAGATATAGG 240 TGATATCGTA AGAGGAAAAG ATCTATATCT CGGTTATGAT AATAAAGAAA AAGAACAAAG 300 AAAAAAATTA GAACAGAAAT TGAAAGATAT TTTCAAGAAA ATACATAAGG ACGTGATGAA 360 GACGAATGGC GCACAAGAAC GCTACATAGA TGATGCCAAA GGAGGAGATT TTTTTCAATT 420 AAGAGAAGAT TGGTGGACGT CGAATCGAGA AACAGTATGG AAAGCATTAA TATGTCATGC 480 ACCAAAAGAA GCTAATTATT TTATAAAAAC AGCGTGTAAT GTAGGAAAAG GAACTAATGG 540 TCAATGCCAT TGCATTGGTG GAGATGTTCC CACATATTTC GATTATGTGC CGCAGTATCT 600 TCGCTGGTTC GAGGAATGGG CAGAAGACTT TTGCAGGAAA AAAAAAAAAA AACTAGAAAA 660 TTTGCAAAAA CAGTGTCGTG ATTACGAACA AAATTTATAT TGTAGTGGTA ATGGCTACGA 720 TTGCACAAAA ACTATATATA AAAAAGGTAA ACTTGTTATA GGTGAACATT GTACAAACTG 780 TTCTGTTTGG TGTCGTATGT ATGAAACTTG GATAGATAAC CAGAAAAAAG AATTTCTAAA 840 ACAAAAAAGA AAATACGAAA CAGAAATATC AGGTGGTGGT AGTGGTAAGA GTCCTAAAAG 900 GACAAAACGG GCTGCACGTA GTAGTAGTAG TAGTGATGAT AATGGGTATG AAAGTAAATT 960 TTATAAAAAA CTGAAAGAAG TTGGCTACCA AGATGTCGAT AAATTTTTAA AAATATTAAA 1020 CAAAGAAGGA ATATGTCAAA AACAACCTCA AGTAGGAAAT GAAAAAGCAG ATAATGTTGA 1080 TTTTACTAAT GAAAAATATG TAAAAACATT TTCTCGTACA GAAATTTGTG AACCGTGCCC 1140 ATGGTGTGGA TTGGAAAAAG GTGGTCCACC ATGGAAAGTT AAAGGTGACA AAACCTGCGG 1200 AAGTGCAAAA ACAAAGACAT ACGATCCTAA AAATATTACC GATATACCAG TACTCTACCC 1260 TGATAAATCA CAGCAAAATA TACTAAAAAA ATATAAAAAT TTTTGTGAAA AAGGTGCACC 1320 TGGTGGTGGT CAAATTAAAA AATGGCAATG TTATTATGAT GAACATAGGC CTAGTAGTAA 1380 AAATAATAAT AATTGTGTAG AAGGAACATG GGACAAGTTT ACACAAGGTA AACAAACCGT 1440 TAAGTCCTAT AATGTTTTTT TTTGGGATTG GGTTCATGAT ATGTTACACG ATTCTGTAGA 1500 GTGGAAGACA GAACTTAGTA AGTGTATAAA TAATAACACT AATGGCAACA CATGTAGAAA 1560 CAATAATAAA TGTAAAACAG ATTGTGGTTG TTTTCAAAAA TGGGTTGAAA AAAAACAACA 1620 AGAATGGATG GCAATAAAAG ACCATTTTGG AAAGCAAACA GATATTGTCC AACAAAAAGG 1680 TCTTATCGTA TTTAGTCCCT ATGGAGTTCT TGACCTTGTT TTGAAGGGCG GTAATCTGTT 1740 GCAAAATATT AAAGATGTTC ATGGAGATAC AGATGACATA AAACACATTA AGAAACTGTT 1800 GGATGAGGAA GACGCAGTAG CAGTTGTTCT TGGTGGCAAG GACAATACCA CAATTGATAA 1860 ATTACTACAA CACGAAAAAG AACAAGCAGA ACAATGCAAA CAAAAGCAGG AAGAATGCGA 1920 GAAAAAAGCA CAACAAGAAA GTCGTGGTCG CTCCGCCGAA ACCCGCGAAG ACGAAAGGAC 1980 ACAACAACCT GCTGATAGTG CCGGCGAAGT CGAAGAAGAA GAAGACGACG ACGACTACGA 2040 CGAAGACGAC GAAGATGACG ACGTAGTCCA GGACGTAGAT GTAAGTGAAA TAAGAGGTCC 2100 G 2101 (2) INFORMATION FOR SEQ ID NO:10: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 700 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Plasmodium falciparum (xi) SEQUENCE DESCRIPTION: SEQ ID NO:10: Glu Gin Gly Asp Asn Lys Val Gly Ala Cys Ala Pro Tyr Arg Arg Leu 1 5 10 15 His Leu Cys Asp Tyr Asn Leu Glu Ser He Asp Thr Thr Ser Thr Thr 20 25 30 His Lys Leu Leu Leu Glu Val Cys Met Ala Ala Lys Tyr Glu Gly Asn 35 40 45 Ser He Asn Thr His Tyr Thr Gin His Gin Arg Thr Asn Glu Asp Ser 50 55 60 Ala Ser Gin Leu Cys Thr Val Leu Ala Arg Ser Phe Ala Asp He Gly 65 70 75 80 Asp He Val Arg Gly Lys Asp Leu Tyr Leu Gly Tyr Asp Asn Lys Glu 85 90 95 Lys Glu Gin Arg Lys Lys Leu Glu Gin Lys Leu Lys Asp He Phe Lys 100 105 110 Lys He His Lys Asp Val Met Lys Thr Asn Gly Ala Gin Glu Arg Tyr 115 120 125 He Asp Asp Ala Lys Gly Gly Asp Phe Phe Gin Leu Arg Glu Asp Trp 130 135 140 Trp Thr Ser Asn Arg Glu Thr Val Trp Lys Ala Leu He Cys His Ala 145 150 155 160 Pro Lys Glu Ala Asn Tyr Phe He Lys Thr Ala Cys Asn Val Gly Lys 165 170 175 Gly Thr Asn Gly Gin Cys His Cys He Gly Gly Asp Val Pro Thr Tyr 180 185 190 Phe Asp Tyr Val Pro Gin Tyr Leu Arg Trp Phe Glu Glu Trp Ala Glu 195 200 205 Asp Phe Cys Arg Lys Lys Lys Lys Lys Leu Glu Asn Leu Gin Lys Gin 210 215 220 Cys Arg Asp Tyr Glu Gin Asn Leu Tyr Cys Ser Gly Asn Gly Tyr Asp 225 230 235 240 Cys Thr Lys Thr He Tyr Lys Lys Gly Lys Leu Val He Gly Glu His 245 250 255 Cys Thr Asn Cys Ser Val Trp Cys Arg Met Tyr Glu Thr Trp He Asp 260 265 270 Asn Gin Lys Lys Glu Phe Leu Lys Gin Lys Arg Lys Tyr Glu Thr Glu 275 280 285 He Ser Gly Gly Gly Ser Gly Lys Ser Pro Lys Arg Thr Lys Arg Ala 290 295 300 Ala Arg Ser Ser Ser Ser Ser Asp Asp Asn Gly Tyr Glu Ser Lys Phe 305 310 315 320 Tyr Lys Lys Leu Lys Glu Val Gly Tyr Gin Asp Val Asp Lys Phe Leu 325 330 335 Lys He Leu Asn Lys Glu Gly He Cys Gin Lys Gin Pro Gin Val Gly 340 345 350 Asn Glu Lys Ala Asp Asn Val Asp Phe Thr Asn Glu Lys Tyr Val Lys 355 360 365 Thr Phe Ser Arg Thr Glu He Cys Glu Pro Cys Pro Trp Cys Gly Leu 370 375 380 Glu Lys Gly Gly Pro Pro Trp Lys Val Lys Gly Asp Lys Thr Cys Gly 385 390 395 400 Ser Ala Lys Thr Lys Thr Tyr Asp Pro Lys Asn He Thr Asp He Pro 405 410 415 Val Leu Tyr Pro Asp Lys Ser Gin Gin Asn He Leu Lys Lys Tyr Lys 420 425 430 Asn Phe Cys Glu Lys Gly Ala Pro Gly Gly Gly Gin He Lys Lys Trp 435 440 445 Gin Cys Tyr Tyr Asp Glu His Arg Pro Ser Ser Lys Asn Asn Asn Asn 450 455 460 Cys Val Glu Gly Thr Trp Asp Lys Phe Thr Gin Gly Lys Gin Thr Val 465 470 475 480 Lys Ser Tyr Asn Val Phe Phe Trp Asp Trp Val His Asp Met Leu His 485 490 495 Asp Ser Val Glu Trp Lys Thr Glu Leu Ser Lys Cys He Asn Asn Asn 500 505 510 Thr Asn Gly Asn Thr Cys Arg Asn Asn Asn Lys Cys Lys Thr Asp Cys 515 520 525 Gly Cys Phe Gin Lys Trp Val Glu Lys Lys Gin Gin Glu Trp Met Ala 530 535 540 He Lys Asp His Phe Gly Lys Gin Thr Asp He Val Gin Gin Lys Gly 545 550 555 560 Leu He Val Phe Ser Pro Tyr Gly Val Leu Asp Leu Val Leu Lys Gly 565 570 575 Gly Asn Leu Leu Gin Asn He Lys Asp Val His Gly Asp Thr Asp Asp 580 585 590 He Lys His He Lys Lys Leu Leu Asp Glu Glu Asp Ala Val Ala Val 595 600 605 Val Leu Gly Gly Lys Asp Asn Thr Thr He Asp Lys Leu Leu Gin His 610 615 620 Glu Lys Glu Gin Ala Glu Gin Cys Lys Gin Lys Gin Glu Glu Cys Glu 625 630 635 640 Lys Lys Ala Gin Gin Glu Ser Arg Gly Arg Ser Ala Glu Thr Arg Glu 645 650 655 Asp Glu Arg Thr Gin Gin Pro Ala Asp Ser Ala Gly Glu Val Glu Glu 660 665 670 Glu Glu Asp Asp Asp Asp Tyr Asp Glu Asp Asp Glu Asp Asp Asp Val 675 680 685 Val Gin Asp Val Asp Val Ser Glu He Arg Gly Pro 690 695 700 (2) INFORMATION FOR SEQ ID NO:11: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8220 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (iii) HYPOTHETICAL: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Plasmodium falciparum (xi) SEQUENCE DESCRIPTION: SEQ ID NO:11: AAAAATGGGG CCCAAGGAGG CTGCAGGTGG GGATGATATT GAGGATGAAA GTGCCAAACA 60 TATGTTTGAT AGGATAGGAA AAGATGTGTA CGATAAAGTA AAAGAGGAAG CTAAAGAACG 120 TGGTAAAGGC TTGCAAGGAC GTTTGTCAGA AGCAAAATTT GAGAAAAATG AAAGCGATCC 180 ACAAACACCA GAAGATCCAT GCGATCTTGA TCATAAATAT CATACAAATG TAACTACTAA 240 TGTAATTAAT CCGTGCGCTG ATAGATCTGA CGTGCGTTTT TCCGATGAAT ATGGAGGTCA 300 ATGTACACAT AATAGAATAA AAGATAGTCA ACAGGGTGAT AATAAAGGTG CATGTGCTCC 360 ATATAGGCGA TTGCATGTAT GCGATCAAAA TTTAGAACAG ATAGAGCCTA TAAAAATAAC 420 AAATACTCAT AATTTATTGG TAGATGTGTG TATGGCAGCA AAATTTGAAG GACAATCAAT 480 AACACAAGAT TATCCAAAAT ATCAAGCAAC ATATGGTGAT TCTCCTTCTC AAATATGTAC 540 TATGCTGGCA CGAAGTTTTG CGGACATAGG GGACATTGTC AGAGGAAGAG ATTTGTATTT 600 AGGTAATCCA CAAGAAATAA AACAAAGACA ACAATTAGAA AATAATTTGA AAACAATTTT 660 CGGGAAAATA TATGAAAAAT TGAATGGCGC AGAAGCACGC TACGGAAATG ATCCGGAATT 720 TTTTAAATTA CGAGAAGATT GGTGGACTGC TAATCGAGAA ACAGTATGGA AAGCCATCAC 780 ATGTAACGCT TGGGGTAATA CATATTTTCA TGCAACGTGC AATAGAGGAG AACGAACTAA 840 AGGTTACTGC CGGTGTAACG ACGACCAAGT TCCCACATAT TTTGATTATG TGCCGCAGTA 900 TCTTCGCTGG TTCGAGGAAT GGGCAGAAGA TTTTTGTAGG AAAAAAAATA AAAAAATAAA 960 AGATGTTAAA AGAAATTGTC GTGGAAAAGA TAAAGAGGAT AAGGATCGAT ATTGTAGCCG 1020 TAATGGCTAC GATTGCGAAA AAACTAAACG AGCGATTGGT AAGTTGCGTT ATGGTAAGCA 1080 ATGCATTAGC TGTTTGTATG CATGTAATCC TTACGTTGAT TGGATAAATA ACCAAAAAGA 1140 ACAATTTGAC AAACAGAAAA AAAAATATGA TGAAGAAATA AAAAAATATG AAAATGGAGC 1200 ATCAGGTGGT AGTAGGCAAA AACGGGATGC AGGTGGTACA ACTACTACTA ATTATGATGG 1260 ATATGAAAAA AAATTTTATG ACGAACTTAA TAAAAGTGAA TATAGAACCG TTGATAAATT 1320 TTTGGAAAAA TTAAGTAATG AAGAAATATG CACAAAAGTT AAAGACGAAG AAGGAGGAAC 1380 AATTGATTTT AAAAACGTTA ATAGTGATAG TACTAGTGGT GCTAGTGGCA CTAATGTTGA 1440 AAGTCAAGGA ACATTTTATC GTTCAAAATA TTGCCAACCC TGCCCTTATT GTGGAGTGAA 1500 AAAGGTAAAT AATGGTGGTA GTAGTAATGA ATGGGAAGAG AAAAATAATG GCAAGTGCAA 1560 GAGTGGAAAA CTTTATGAGC CTAAACCCGA CAAAGAAGGT ACTACTATTA CAATCCTTAA 1620 AAGTGGTAAA GGACATGATG ATATTGAAGA AAAATTAAAC AAATTTTGTG ATGAAAAAAA 1680 TGGTGATACA ATAAATAGTG GTGGTAGTGG TACGGGTGGT AGTGGTGGTG GTAACAGTGG 1740 TAGACAGGAA TTGTATGAAG AATGGAAATG TTATAAAGGT GAAGATGTAG TGAAAGTTGG 1800 ACACGATGAG GATGACGAGG AGGATTATGA AAATGTAAAA AATGCAGGCG GATTATGTAT 1860 ATTAAAAAAC CAAAAAAAGA ATAAAGAAGA AGGTGGAAAT ACGTCTGAAA AGGAGCCTGA 1920 TGAAATCCAA AAGACATTCA ATCCTTTTTT TTACTATTGG GTTGCACATA TGTTAAAAGA 1980 TTCCATACAT TGGAAAAAAA AACTTCAGAG ATGTTTACAA AATGGTAACA GAATAAAATG 2040 TGGAAACAAT AAATGTAATA ATGATTGTGA ATGTTTTAAA AGATGGATTA CACAAAAAAA 2100 AGACGAATGG GGGAAAATAG TACAACATTT TAAAACGCAA AATATTAAAG GTAGAGGAGG 2160 TAGTGACAAT ACGGCAGAAT TAATCCCATT TGATCACGAT TATGTTCTTC AATACAATTT 2220 GCAAGAAGAA TTTTTGAAAG GCGATTCCGA AGACGCTTCC GAAGAAAAAT CCGAAAATAG 2280 TCTGGATGCA GAGGAGGCAG AGGAACTAAA ACACCTTCGC GAAATCATTG AAAGTGAAGA 2340 CAATAATCAA GAAGCATCTG TTGGTGGTGG CGTCACTGAA CAAAAAAATA TAATGGATAA 2400 ATTGCTCAAC TACGAAAAAG ACGAAGCCGA TTTATGCCTA GAAATTCACG AAGATGAGGA 2460 AGAGGAAAAA GAAAAAGGAG ACGGAAACGA ATGTATCGAA GAGGGCGAAA ATTTTCGTTA 2520 TAATCCATGT AGTGGCGAAA GTGGTAACAA ACGATACCCC GTTCTTGCGA ACAAAGTAGC 2580 GTATCAAATG CATCACAAGG CAAAGACACA ATTGGCTAGT CGTGCTGGTA GAAGTGCGTT 2640 GAGAGGTGAT ATATCCTTAG CGCAATTTAA AAATGGTCGT AACGGAAGTA CATTGAAAGG 2700 ACAAATTTGC AAAATTAACG AAAACTATTC CAATGATAGT CGTGGTAATA GTGGTGGACC 2760 ATGTACAGGC AAAGATGGAG ATCACGGAGG TGTGCGCATG AGAATAGGAA CGGAATGGTC 2820 AAATATTGAA GGAAAAAAAC AAACGTCATA CAAAAACGTC TTTTTACCTC CCCGACGAGA 2880 ACACATGTGT ACATCCAATT TAGAAAATTT AGATGTTGGT AGTGTCACTA AAAATGATAA 2940 GGCTAGCCAC TCATTATTGG GAGATGTTCA GCTCGCAGCA AAAACTGATG CAGCTGAGAT 3000 AATAAAACGC TATAAAGATC AAAATAATAT ACAACTAACT GATCCAATAC AACAAAAAGA 3060 CCAGGAGGCT ATGTGTCGAG CTGTACGTTA TAGTTTTGCC GATTTAGGAG ACATTATTCG 3120 AGGAAGAGAT ATGTGGGATG AGGATAAGAG CTCAACAGAC ATGGAAACAC GTTTGATAAC 3180 CGTATTTAAA AACATTAAAG AAAAACATGA TGGAATCAAA GACAACCCTA AATATACCGG 3240 TGATGAAAGC AAAAAGCCCG CATATAAAAA ATTACGAGCA GATTGGTGGG AAGCAAATAG 3300 ACATCAAGTG TGGAGAGCCA TGAAATGCGC AACAAAAGGC ATCATATGTC CTGGTATGCC 3360 AGTTGACGAT TATATCCCCC AACGTTTACG CTGGATGACT GAATGGGCTG AATGGTATTG 3420 TAAAGCGCAA TCACAGGAGT ATGACAAGTT AAAAAAAATC TGTGCAGATT GTATGAGTAA 3480 GGGTGATGGA AAATGTACGC AAGGTGATGT CGATTGTGGA AAGTGCAAAG CAGCATGTGA 3540 TAAATATAAA GAGGAAATAG AAAAATGGAA TGAACAATGG AGAAAAATAT CAGATAAATA 3600 CAATCTATTA TACCTACAAG CAAAAACTAC TTCTACTAAT CCTGGCCGTA CTGTTCTTGG 3660 TGATGACGAT CCCGACTATC AACAAATGGT AGATTTTTTG ACCCCAATAC ACAAAGCAAG 3720 TATTGCCGCA CGTGTTCTTG TTAAACGTGC TGCTGGTAGT CCCACTGAGA TCGCCGCCGC 3780 CGCCCCGATC ACCCCCTACA GTACTGCTGC CGGATATATA CACCAGGAAA TAGGATATGG 3840 GGGGTGCCAG GAACAAACAC AATTTTGTGA AAAAAAACAT GGTGCAACAT CAACTAGTAC 3900 CACGAAAGAA AACAAAGAAT ACACCTTTAA ACAACCTCCG CCGGAGTATG CTACAGCGTG 3960 TGATTGCATA AATAGGTCGC AAACAGAGGA GCCGAAGAAA AAGGAAGAAA ATGTAGAGAG 4020 TGCCTGCAAA ATAGTGGAGA AAATACTTGA GGGTAAGAAT GGAAGGACTA CAGTAGGTGA 4080 ATGTAATCCA AAAGAGAGTT ATCCTGATTG GGATTGCAAA AACAATATTG ACATTAGTCA 4140 TGATGGTGCT TGTATGCCTC CAAGGAGACA AAAACTATGT TTATATTATA TAGCACATGA 4200 GAGTCAAACA GAAAATATAA AAACAGACGA TAATTTGAAA GATGCTTTTA TTAAAACTGC 4260 AGCAGCAGAA ACTTTTCTTT CATGGCAATA TTATAAGAGT AAGAATGATA GTGAAGCTAA 4320 AATATTAGAT AGAGGCCTTA TTCCATCCCA ATTTTTAAGA TCCATGATGT ACACGTTTGG 4380 AGATTATAGA GATATATGTT TGAACACAGA TATATCTAAA AAACAAAATG ATGTAGCTAA 4440 GGCAAAAGAT AAAATAGGTA AATTTTTCTC AAAAGATGGC AGCAAATCTC CTAGTGGCTT 4500 ATCACGCCAA GAATGGTGGA AAACAAATGG TCCAGAGATT TGGAAAGGAA TGTTATGTGC 4560 CTTAACAAAA TACGTCACAG ATACCGATAA CAAAAGAAAA ATCAAAAACG ACTACTCATA 4620 CGATAAAGTC AACCAATCCC AAAATGGCAA CCCTTCCCTT GAAGAGTTTG CTGCTAAACC 4680 TCAATTTCTA CGTTGGATGA TCGAATGGGG AGAAGAGTTT TGTGCTGAAC GTCAGAAGAA 4740 GGAAAATATC ATAAAAGATG CATGTAATGA AATAAATTCT ACACAACAGT GTAATGATGC 4800 GAAACATCGT TGTAATCAAG CATGTAGAGC ATATCAAGAA TATGTTGAAA ATAAAAAAAA 4860 AGAATTTTCG GGACAAACAA ATAACTTTGT TCTAAAGGCA AATGTTCAGC CCCAAGATCC 4920 AGAATATAAA GGATATGAAT ATAAAGACGG CGTACAACCG ATACAGGGGA ATGAGTATTT 4980 ACTGCAAAAA TGTGATAATA ATAAATGTTC TTGCATGGAT GGAAATGTAC TTTCCGTCTC 5040 TCCAAAAGAA AAACCTTTTG GAAAATATGC CCATAAATAT CCTGAGAAAT GTGATTGTTA 5100 TCAAGGAAAA CATGTACCTA GCATACCACC TCCCCCCCCA CCTGTACAAC CACAACCGGA 5160 AGCACCAACA GTAACAGTAG ACGTTTGCAG CATAGTAAAA ACACTATTTA AAGACACAAA 5220 CAATTTTTCC GACGCTTGTG GTCTAAAATA CGGCAAAACC GCACCATCCA GTTGGAAATG 5280 TATACCAAGT GACACAAAAA GTGGTGCTGG TGCCACCACC GGCAAAAGTG GTAGTGATAG 5340 TGGTAGTATT TGTATCCCAC CCAGGAGGCG ACGATTATAT GTGGGGAAAC TACAGGAGTG 5400 GGCTACCGCG CTCCCACAAG GTGAGGGCGC CGCGCCGTCC CACTCACGCG CCGACGACTT 5460 GCGCAATGCG TTCATCCAAT CTGCTGCAAT AGAGACTTTT TTCTTATGGG ATAGATATAA 5520 AGAAGAGAAA AAACCACAGG GTGATGGGTC ACAACAAGCA CTATCACAAC TAACCAGTAC 5580 ATACAGTGAT GACGAGGAGG ACCCCCCCGA CAAACTGTTA CAAAATGGTA AGATACCCCC 5640 CGATTTTTTG AGATTAATGT TCTATACATT AGGAGATTAT AGGGATATTT TAGTACACGG 5700 TGGTAACACA AGTGACAGTG GTAACACAAA TGGTAGTAAC AACAACAATA TTGTGCTTGA 5760 AGCGAGTGGT AACAAGGAGG ACATGCAAAA AATACAAGAG AAAATAGAAC AAATTCTCCC 5820 AAAAAATGGT GGCACACCTC TTGTCCCAAA ATCTAGTGCC CAAACACCTG ATAAATGGTG 5880 GAATGAACAC GCCGAATCTA TCTGGAAAGG TATGATATGT GCATTGACAT ATACAGAAAA 5940 GAACCCTGAC ACCAGTGCAA GAGGCGACGA AAACAAAATA GAAAAGGATG ATGAAGTGTA 6000 CGAGAAATTT TTTGGCAGCA CAGCCGACAA ACATGGCACA GCCTCAACCC CAACCGGCAC 6060 ATACAAAACC CAATACGACT ACGAAAAAGT CAAACTTGAG GATACAAGTG GTGCCAAAAC 6120 CCCCTCAGCC TCTAGTGATA CACCCCTTCT CTCCGATTTC GTGTTACGCC CCCCCTACTT 6180 CCGTTACCTT GAAGAATGGG GTCAAAATTT TTGTAAAAAA AGAAAGCATA AATTGGCACA 6240 AATAAAACAT GAGTGTAAAG TAGAAGAAAA TGGTGGTGGT AGTCGTCGTG GTGGTATAAC 6300 AAGACAATAT AGTGGGGATG GCGAAGCGTG TAATGAGATG CTTCCAAAAA ACGATGGAAC 6360 TGTTCCGGAT TTAGAAAAGC CGAGTTGTGC CAAACCTTGT AGTTCTTATA GAAAATGGAT 6420 AGAAAGCAAG GGAAAAGAGT TTGAGAAACA AGAAAAGGCA TATGAACAAC AAAAAGACAA 6480 ATGTGTAAAT GGAAGTAATA AGCATGATAA TGGATTTTGT GAAACACTAA CAACGTCCTC 6540 TAAAGCTAAA GACTTTTTAA AAACGTTAGG ACCATGTAAA CCTAATAATG TAGAGGGTAA 6600 AACAATTTTT GATGATGATA AAACCTTTAA ACATACAAAA GATTGTGATC CATGTCTTAA 6660 ATTTAGTGTT AATTGTAAAA AAGATGAATG TGATAATTCT AAAGGAACCG ATTGCCGAAA 6720 TAAAAATAGT ATTGATGCAA CAGATATTGA AAATGGAGTG GATTCTACTG TACTAGAAAT 6780 GCGTGTCAGT GCTGATAGTA AAAGTGGATT TAATGGTGAT GGTTTAGAGA ATGCTTGTAG 6840 AGGTGCTGGT ATCTTTGAAG GTATTAGAAA AGATGAATGG AAATGTCGTA ATGTATGTGG 6900 TTATGTTGTA TGTAAACCGG AAAACGTTAA TGGGGAAGCA AAGGGAAAAC ACATTATACA 6960 AATTAGAGCA CTGGTTAAAC GTTGGGTAGA ATATTTTTTT GAAGATTATA ATAAAATAAA 7020 ACATAAAATT TCACATCGCA TAAAAAATGG TGAAATATCT CCATGTATAA AAAATTGTGT 7080 AGAAAAATGG GTAGATCAGA AAAGAAAAGA ATGGAAGGAA ATTACTGAAC GTTTCAAAGA 7140 TCAATATAAA AATGACAATT CAGATGATGA CAATGTGAGA AGTTTTTTGG AGACCTTGAT 7200 ACCTCAAATT ACTGATGCAA ACGCTAAAAA TAAGGTTATA AAATTAAGTA AGTTCGGTAA 7260 TTCTTGTGGA TGTAGTGCCA GTGCGAACGA ACAAAACAAA AATGGTGAAT ACAAGGACGC 7320 TATAGATTGT ATGCTTAAAA AGCTTAAAGA TAAAATTGGC GAGTGCGAAA AGAAACACCA 7380 TCAAACTAGT GATACCGAGT GTTCCGACAC ACCACAACCG CAAACCCTTG AAGACGAAAC 7440 TTTGGATGAT GATATAGAAA CAGAGGAGGC GAAGAAGAAC ATGATGCCGA AAATTTGTGA 7500 AAATGTGTTA AAAACAGCAC AACAAGAGGA TGAAGGCGGT TGTGTCCCAG CAGAAAATAG 7560 TGAAGAACCG GCAGCAACAG ATAGTGGTAA GGAAACCCCC GAACAAACCC CCGTTCTCAA 7620 ACCCGAAGAA GAAGCAGTAC CGGAACCACC ACCTCCACCC CCACAGGAAA AAGCCCCGGC 7680 ACCAATACCC CAACCACAAC CACCAACCCC CCCCACACAA CTCTTGGATA ATCCCCACGT 7740 TCTAACCGCC CTGGTGACCT CCACCCTCGC CTGGAGCGTT GGCATCGGTT TTGCTACATT 7800 CACTTATTTT TATCTAAAGG TAAATGGAAG TATATATATG GGGATGTGGA TGTATGTGGA 7860 TGTATGTGAA TGTATGTGGA TGTATGTGGA TGTATGTGGA TGTGTTTTAT GGATATGTAT 7920 TTGTGATTAT GTTTGGATAT ATATATATAT ATATATATGT TTATGTATAT GTGTTTTTGG 7980 ATATATATAT GTGTATGTAT ATGATTTTCT GTATATGTAT TTGTGGGTTA AGGATATATA 8040 TATATGGATG TACTTGTATG TGTTTTATAT ATATATTTTA TATATATGTA TTTATATTAA 8100 AAAAGAAATA TAAAAACAAA TTTATTAAAA TGAAAAAAAG AAAAATGAAA TATAAAAAAA 8160 AATTTATTAA AATAAAAAAA AAAAAAAAAA AAAAGGAGAA AAATTTTTTA AAAAATAATA 8220 (2) INFORMATION FOR SEQ ID NO:12: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2710 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Plasmodium falciparum ( i) SEQUENCE DESCRIPTION: SEQ ID NO:12: Asn Val Met Val Glu Leu Ala Lys Met Gly Pro Lys Glu Ala Ala Gly 1 5 10 15 Gly Asp Asp He Glu Asp Glu Ser Ala Lys His Met Phe Asp Arg He 20 25 30 Gly Lys Asp Val Tyr Asp Lys Val Lys Glu Glu Ala Lys Glu Arg Gly 35 40 45 Lys Gly Leu Gin Gly Arg Leu Ser Glu Ala Lys Phe Glu Lys Asn Glu 50 55 60 Ser Asp Pro Gin Thr Pro Glu Asp Pro Cys Asp Leu Asp His Lys Tyr 65 70 75 80 His Thr Asn Val Thr Thr Asn Val He Asn Pro Cys Ala Asp Arg Ser 85 90 95 Asp Val Arg Phe Ser Asp Glu Tyr Gly Gly Gin Cys Thr His Asn Arg 100 105 110 He Lys Asp Ser Gin Gin Gly Asp Asn Lys Gly Ala Cys Ala Pro Tyr 115 120 125 Arg Arg Leu His Val Cys Asp Gin Asn Leu Glu Gin He Glu Pro He 130 135 140 Lys He Thr Asn Thr His Asn Leu Leu Val Asp Val Cys Met Ala Ala 145 150 155 160 Lys Phe Glu Gly Gin Ser He Thr Gin Asp Tyr Pro Lys Tyr Gin Ala 165 170 175 Thr Tyr Gly Asp Ser Pro Ser Gin He Cys Thr Met Leu Ala Arg Ser 180 185 190 Phe Ala Asp He Gly Asp He Val Arg Gly Arg Asp Leu Tyr Leu Gly 195 200 205 Asn Pro Gin Glu He Lys Gin Arg Gin Gin Leu Glu Asn Asn Leu Lys 210 215 220 Thr He Phe Gly Lys He Tyr Glu Lys Leu Asn Gly Ala Glu Ala Arg 225 230 235 240 Tyr Gly Asn Asp Pro Glu Phe Phe Lys Leu Arg Glu Asp Trp Trp Thr 245 250 255 Ala Asn Arg Glu Thr Val Trp Lys Ala He Thr Cys Asn Ala Trp Gly 260 265 270 Asn Thr Tyr Phe His Ala Thr Cys Asn Arg Gly Glu Arg Thr Lys Gly 275 280 285 Tyr Cys Arg Cys Asn Asp Asp Gin Val Pro Thr Tyr Phe Asp Tyr Val 290 295 300 Pro Gin Tyr Leu Arg Trp Phe Glu Glu Trp Ala Glu Asp Phe Cys Arg 305 310 315 320 Lys Lys Asn Lys Lys He Lys Asp Val Lys Arg Asn Cys Arg Gly Lys 325 330 335 Asp Lys Glu Asp Lys Asp Arg Tyr Cys Ser Arg Asn Gly Tyr Asp Cys 340 345 350 Glu Lys Thr Lys Arg Ala He Gly Lys Leu Arg Tyr Gly Lys Gin Cys 355 360 365 He Ser Cys Leu Tyr Ala Cys Asn Pro Tyr Val Asp Trp He Asn Asn 370 375 380 Gin Lys Glu Gin Phe Asp Lys Gin Lys Lys Lys Tyr Asp Glu Glu He 385 390 395 400 Lys Lys Tyr Glu Asn Gly Ala Ser Gly Gly Ser Arg Gin Lys Arg Asp 405 410 415 Ala Gly Gly Thr Thr Thr Thr Asn Tyr Asp Gly Tyr Glu Lys Lys Phe 420 425 430 Tyr Asp Glu Leu Asn Lys Ser Glu Tyr Arg Thr Val Asp Lys Phe Leu 435 440 445 Glu Lys Leu Ser Asn Glu Glu He Cys Thr Lys Val Lys Asp Glu Glu 450 455 460 Gly Gly Thr He Asp Phe Lys Asn Val Asn Ser Asp Ser Thr Ser Gly 465 470 475 480 Ala Ser Gly Thr Asn Val Glu Ser Gin Gly Thr Phe Tyr Arg Ser Lys 485 490 495 Tyr Cys Gin Pro Cys Pro Tyr Cys Gly Val Lys Lys Val Asn Asn Gly 500 505 510 Gly Ser Ser Asn Glu Trp Glu Glu Lys Asn Asn Gly Lys Cys Lys Ser 515 520 525 Gly Lys Leu Tyr Glu Pro Lys Pro Asp Lys Glu Gly Thr Thr He Thr 530 535 540 He Leu Lys Ser Gly Lys Gly His Asp Asp He Glu Glu Lys Leu Asn 545 550 555 560 Lys Phe Cys Asp Glu Lys Asn Gly Asp Thr He Asn Ser Gly Gly Ser 565 570 575 Gly Thr Gly Gly Ser Gly Gly Gly Asn Ser Gly Arg Gin Glu Leu Tyr 580 585 590 Glu Glu Trp Lys Cys Tyr Lys Gly Glu Asp Val Val Lys Val Gly His 595 600 605 Asp Glu Asp Asp Glu Glu Asp Tyr Glu Asn Val Lys Asn Ala Gly Gly 610 615 620 Leu Cys He Leu Lys Asn Gin Lys Lys Asn Lys Glu Glu Gly Gly Asn 625 630 635 640 Thr Ser Glu Lys Glu Pro Asp Glu He Gin Lys Thr Phe Asn Pro Phe 645 650 655 Phe Tyr Tyr Trp Val Ala His Met Leu Lys Asp Ser He His Trp Lys 660 665 670 Lys Lys Leu Gin Arg Cys Leu Gin Asn Gly Asn Arg He Lys Cys Gly 675 680 685 Asn Asn Lys Cys Asn Asn Asp Cys Glu Cys Phe Lys Arg Trp He Thr 690 695 700 Gin Lys Lys Asp Glu Trp Gly Lys He Val Gin His Phe Lys Thr Gin 705 710 715 720 Asn He Lys Gly Arg Gly Gly Ser Asp Asn Thr Ala Glu Leu He Pro 725 730 735 Phe Asp His Asp Tyr Val Leu Gin Tyr Asn Leu Gin Glu Glu Phe Leu 740 745 750 Lys Gly Asp Ser Glu Asp Ala Ser Glu Glu Lys Ser Glu Asn Ser Leu 755 760 765 Asp Ala Glu Glu Ala Glu Glu Leu Lys His Leu Arg Glu He He Glu 770 775 780 Ser Glu Asp Asn Asn Gin Glu Ala Ser Val Gly Gly Gly Val Thr Glu 785 790 795 800 Gin Lys Asn He Met Asp Lys Leu Leu Asn Tyr Glu Lys Asp Glu Ala 805 810 815 Asp Leu Cys Leu Glu He His Glu Asp Glu Glu Glu Glu Lys Glu Lys 820 825 830 Gly Asp Gly Asn Glu Cys He Glu Glu Gly Glu Asn Phe Arg Tyr Asn 835 840 845 Pro Cys Ser Gly Glu Ser Gly Asn Lys Arg Tyr Pro Val Leu Ala Asn 850 855 860 Lys Val Ala Tyr Gin Met His His Lys Ala Lys Thr Gin Leu Ala Ser 865 870 875 880 Arg Ala Gly Arg Ser Ala Leu Arg Gly Asp He Ser Leu Ala Gin Phe 885 890 895 Lys Asn Gly Arg Asn Gly Ser Thr Leu Lys Gly Gin He Cys Lys He 900 905 910 Asn Glu Asn Tyr Ser Asn Asp Ser Arg Gly Asn Ser Gly Gly Pro Cys 915 920 925 Thr Gly Lys Asp Gly Asp His Gly Gly Val Arg Met Arg He Gly Thr 930 935 940 Glu Trp Ser Asn He Glu Gly Lys Lys Gin Thr Ser Tyr Lys Asn Val 945 950 955 960 Phe Leu Pro Pro Arg Arg Glu His Met Cys Thr Ser Asn Leu Glu Asn 965 970 975 Leu Asp Val Gly Ser Val Thr Lys Asn Asp Lys Ala Ser His Ser Leu 980 985 990 Leu Gly Asp Val Gin Leu Ala Ala Lys Thr Asp Ala Ala Glu He He 995 1000 1005 Lys Arg Tyr Lys Asp Gin Asn Asn He Gin Leu Thr Asp Pro He Gin 1010 1015 1020 Gin Lys Asp Gin Glu Ala Met Cys Arg Ala Val Arg Tyr Ser Phe Ala 1025 1030 1035 1040 Asp Leu Gly Asp He He Arg Gly Arg Asp Met Trp Asp Glu Asp Lys 1045 1050 1055 Ser Ser Thr Asp Met Glu Thr Arg Leu He Thr Val Phe Lys Asn He 1060 1065 1070 Lys Glu Lys His Asp Gly He Lys Asp Asn Pro Lys Tyr Thr Gly Asp 1075 1080 1085 Glu Ser Lys Lys Pro Ala Tyr Lys Lys Leu Arg Ala Asp Trp Trp Glu 1090 1095 1100 Ala Asn Arg His Gin Val Trp Arg Ala Met Lys Cys Ala Thr Lys Gly 1105 1110 1115 1120 He He Cys Pro Gly Met Pro Val Asp Asp Tyr He Pro Gin Arg Leu 1125 1130 1135 Arg Trp Met Thr Glu Trp Ala Glu Trp Tyr Cys Lys Ala Gin Ser Gin 1140 1145 1150 Glu Tyr Asp Lys Leu Lys Lys He Cys Ala Asp Cys Met Ser Lys Gly 1155 1160 1165 Asp Gly Lys Cys Thr Gin Gly Asp Val Asp Cys Gly Lys Cys Lys Ala 1170 1175 1180 Ala Cys Asp Lys Tyr Lys Glu Glu He Glu Lys Trp Asn Glu Gin Trp 1185 1190 1195 1200 Arg Lys He Ser Asp Lys Tyr Asn Leu Leu Tyr Leu Gin Ala Lys Thr 1205 1210 1215 Thr Ser Thr Asn Pro Gly Arg Thr Val Leu Gly Asp Asp Asp Pro Asp 1220 1225 1230 Tyr Gin Gin Met Val Asp Phe Leu Thr Pro He His Lys Ala Ser He 1235 1240 1245 Ala Ala Arg Val Leu Val Lys Arg Ala Ala Gly Ser Pro Thr Glu He 1250 1255 1260 Ala Ala Ala Ala Pro He Thr Pro Tyr Ser Thr Ala Ala Gly Tyr He 1265 1270 1275 1280 His Gin Glu He Gly Tyr Gly Gly Cys Gin Glu Gin Thr Gin Phe Cys 1285 1290 1295 Glu Lys Lys His Gly Ala Thr Ser Thr Ser Thr Thr Lys Glu Asn Lys 1300 1305 1310 Glu Tyr Thr Phe Lys Gin Pro Pro Pro Glu Tyr Ala Thr Ala Cys Asp 1315 1320 1325 Cys He Asn Arg Ser Gin Thr Glu Glu Pro Lys Lys Lys Glu Glu Asn 1330 1335 1340 Val Glu Ser Ala Cys Lys He Val Glu Lys He Leu Glu Gly Lys Asn 1345 1350 1355 1360 Gly Arg Thr Thr Val Gly Glu Cys Asn Pro Lys Glu Ser Tyr Pro Asp 1365 1370 1375 Trp Asp Cys Lys Asn Asn He Asp He Ser His Asp Gly Ala Cys Met 1380 1385 1390 Pro Pro Arg Arg Gin Lys Leu Cys Leu Tyr Tyr He Ala His Glu Ser 1395 1400 1405 Gin Thr Glu Asn He Lys Thr Asp Asp Asn Leu Lys Asp Ala Phe He 1410 1415 1420 Lys Thr Ala Ala Ala Glu Thr Phe Leu Ser Trp Gin Tyr Tyr Lys Ser 1425 1430 1435 1440 Lys Asn Asp Ser Glu Ala Lys He Leu Asp Arg Gly Leu He Pro Ser 1445 1450 1455 Gin Phe Leu Arg Ser Met Met Tyr Thr Phe Gly Asp Tyr Arg Asp He 1460 1465 1470 Cys Leu Asn Thr Asp He Ser Lys Lys Gin Asn Asp Val Ala Lys Ala 1475 1480 1485 Lys Asp Lys He Gly Lys Phe Phe Ser Lys Asp Gly Ser Lys Ser Pro 1490 1495 1500 Ser Gly Leu Ser Arg Gin Glu Trp Trp Lys Thr Asn Gly Pro Glu He 1505 1510 1515 1520 Trp Lys Gly Met Leu Cys Ala Leu Thr Lys Tyr Val Thr Asp Thr Asp 1525 1530 1535 Asn Lys Arg Lys He Lys Asn Asp Tyr Ser Tyr Asp Lys Val Asn Gin 1540 1545 1550 Ser Gin Asn Gly Asn Pro Ser Leu Glu Glu Phe Ala Ala Lys Pro Gin 1555 1560 1565 Phe Leu Arg Trp Met He Glu Trp Gly Glu Glu Phe Cys Ala Glu Arg 1570 1575 1580 Gin Lys Lys Glu Asn He He Lys Asp Ala Cys Asn Glu He Asn Ser 1585 1590 1595 1600 Thr Gin Gin Cys Asn Asp Ala Lys His Arg Cys Asn Gin Ala Cys Arg 1605 1610 1615 Ala Tyr Gin Glu Tyr Val Glu Asn Lys Lys Lys Glu Phe Ser Gly Gin 1620 1625 1630 Thr Asn Asn Phe Val Leu Lys Ala Asn Val Gin Pro Gin Asp Pro Glu 1635 1640 1645 Tyr Lys Gly Tyr Glu Tyr Lys Asp Gly Val Gin Pro He Gin Gly Asn 1650 1655 1660 Glu Tyr Leu Leu Gin Lys Cys Asp Asn Asn Lys Cys Ser Cys Met Asp 1665 1670 1675 1680 Gly Asn Val Leu Ser Val Ser Pro Lys Glu Lys Pro Phe Gly Lys Tyr 1685 1690 1695 Ala His Lys Tyr Pro Glu Lys Cys Asp Cys Tyr Gin Gly Lys His Val 1700 1705 1710 Pro Ser He Pro Pro Pro Pro Pro Pro Val Gin Pro Gin Pro Glu Ala 1715 1720 1725 Pro Thr Val Thr Val Asp Val Cys Ser He Val Lys Thr Leu Phe Lys 1730 1735 1740 Asp Thr Asn Asn Phe Ser Asp Ala Cys Gly Leu Lys Tyr Gly Lys Thr 1745 1750 1755 1760 Ala Pro Ser Ser Trp Lys Cys He Pro Ser Asp Thr Lys Ser Gly Ala 1765 1770 1775 Gly Ala Thr Thr Gly Lys Ser Gly Ser Asp Ser Gly Ser He Cys He 1780 1785 1790 Pro Pro Arg Arg Arg Arg Leu Tyr Val Gly Lys Leu Gin Glu Trp Ala 1795 1800 1805 Thr Ala Leu Pro Gin Gly Glu Gly Ala Ala Pro Ser His Ser Arg Ala 1810 1815 1820 Asp Asp Leu Arg Asn Ala Phe He Gin Ser Ala Ala He Glu Thr Phe 1825 1830 1835 1840 Phe Leu Trp Asp Arg Tyr Lys Glu Glu Lys Lys Pro Gin Gly Asp Gly 1845 1850 1855 Ser Gin Gin Ala Leu Ser Gin Leu Thr Ser Thr Tyr Ser Asp Asp Glu 1860 1865 1870 Glu Asp Pro Pro Asp Lys Leu Leu Gin Asn Gly Lys He Pro Pro Asp 1875 1880 1885 Phe Leu Arg Leu Met Phe Tyr Thr Leu Gly Asp Tyr Arg Asp He Leu 1890 1895 1900 Val His Gly Gly Asn Thr Ser Asp Ser Gly Asn Thr Asn Gly Ser Asn 1905 1910 1915 1920 Asn Asn Asn He Val Leu Glu Ala Ser Gly Asn Lys Glu Asp Met Gin 1925 1930 1935 Lys He Gin Glu Lys He Glu Gin He Leu Pro Lys Asn Gly Gly Thr 1940 1945 1950 Pro Leu Val Pro Lys Ser Ser Ala Gin Thr Pro Asp Lys Trp Trp Asn 1955 1960 1965 Glu His Ala Glu Ser He Trp Lys Gly Met He Cys Ala Leu Thr Tyr 1970 1975 1980 Thr Glu Lys Asn Pro Asp Thr Ser Ala Arg Gly Asp Glu Asn Lys He 1985 1990 1995 2000 Glu Lys Asp Asp Glu Val Tyr Glu Lys Phe Phe Gly Ser Thr Ala Asp 2005 2010 2015 Lys His Gly Thr Ala Ser Thr Pro Thr Gly Thr Tyr Lys Thr Gin Tyr 2020 2025 2030 Asp Tyr Glu Lys Val Lys Leu Glu Asp Thr Ser Gly Ala Lys Thr Pro 2035 2040 2045 Ser Ala Ser Ser Asp Thr Pro Leu Leu Ser Asp Phe Val Leu Arg Pro 2050 2055 2060 Pro Tyr Phe Arg Tyr Leu Glu Glu Trp Gly Gin Asn Phe Cys Lys Lys 2065 2070 2075 2080 Arg Lys His Lys Leu Ala Gin He Lys His Glu Cys Lys Val Glu Glu 2085 2090 2095 Asn Gly Gly Gly Ser Arg Arg Gly Gly He Thr Arg Gin Tyr Ser Gly 2100 2105 2110 Asp Gly Glu Ala Cys Asn Glu Met Leu Pro Lys Asn Asp Gly Thr Val 2115 2120 2125 Pro Asp Leu Glu Lys Pro Ser Cys Ala Lys Pro Cys Ser Ser Tyr Arg 2130 2135 2140 Lys Trp He Glu Ser Lys Gly Lys Glu Phe Glu Lys Gin Glu Lys Ala 2145 2150 2155 2160 Tyr Glu Gin Gin Lys Asp Lys Cys Val Asn Gly Ser Asn Lys His Asp 2165 2170 2175 Asn Gly Phe Cys Glu Thr Leu Thr Thr Ser Ser Lys Ala Lys Asp Phe 2180 2185 2190 Leu Lys Thr Leu Gly Pro Cys Lys Pro Asn Asn Val Glu Gly Lys Thr 2195 2200 2205 He Phe Asp Asp Asp Lys Thr Phe Lys His Thr Lys Asp Cys Asp Pro 2210 2215 2220 Cys Leu Lys Phe Ser Val Asn Cys Lys Lys Asp Glu Cys Asp Asn Ser 2225 2230 2235 2240 Lys Gly Thr Asp Cys Arg Asn Lys Asn Ser He Asp Ala Thr Asp He 2245 2250 2255 Glu Asn Gly Val Asp Ser Thr Val Leu Glu Met Arg Val Ser Ala Asp 2260 2265 2270 Ser Lys Ser Gly Phe Asn Gly Asp Gly Leu Glu Asn Ala Cys Arg Gly 2275 2280 2285 Ala Gly He Phe Glu Gly He Arg Lys Asp Glu Trp Lys Cys Arg Asn 2290 2295 2300 Val Cys Gly Tyr Val Val Cys Lys Pro Glu Asn Val Asn Gly Glu Ala 2305 2310 2315 2320 Lys Gly Lys His He He Gin He Arg Ala Leu Val Lys Arg Trp Val 2325 2330 2335 Glu Tyr Phe Phe Glu Asp Tyr Asn Lys He Lys His Lys He Ser His 2340 2345 2350 Arg He Lys Asn Gly Glu He Ser Pro Cys He Lys Asn Cys Val Glu 2355 2360 2365 Lys Trp Val Asp Gin Lys Arg Lys Glu Trp Lys Glu He Thr Glu Arg 2370 2375 2380 Phe Lys Asp Gin Tyr Lys Asn Asp Asn Ser Asp Asp Asp Asn Val Arg 2385 2390 2395 2400 Ser Phe Leu Glu Thr Leu He Pro Gin He Thr Asp Ala Asn Ala Lys 2405 2410 2415 Asn Lys Val He Lys Leu Ser Lys Phe Gly Asn Ser Cys Gly Cys Ser 2420 2425 2430 Ala Ser Ala Asn Glu Gin Asn Lys Asn Gly Glu Tyr Lys Asp Ala He 2435 2440 2445 Asp Cys Met Leu Lys Lys Leu Lys Asp Lys He Gly Glu Cys Glu Lys 2450 2455 2460 Lys His His Gin Thr Ser Asp Thr Glu Cys Ser Asp Thr Pro Gin Pro 2465 2470 2475 2480 Gin Thr Leu Glu Asp Glu Thr Leu Asp Asp Asp He Glu Thr Glu Glu 2485 2490 2495 Ala Lys Lys Asn Met Met Pro Lys He Cys Glu Asn Val Leu Lys Thr 2500 2505 2510 Ala Gin Gin Glu Asp Glu Gly Gly Cys Val Pro Ala Glu Asn Ser Glu 2515 2520 2525 Glu Pro Ala Ala Thr Asp Ser Gly Lys Glu Thr Pro Glu Gin Thr Pro 2530 2535 2540 Val Leu Lys Pro Glu Glu Glu Ala Val Pro Glu Pro Pro Pro Pro Pro 2545 2550 2555 2560 Pro Gin Glu Lys Ala Pro Ala Pro He Pro Gin Pro Gin Pro Pro Thr 2565 2570 2575 Pro Pro Thr Gin Leu Leu Asp Asn Pro His Val Leu Thr Ala Leu Val 2580 2585 2590 Thr Ser Thr Leu Ala Trp Ser Val Gly He Gly Phe Ala Thr Phe Thr 2595 2600 2605 Tyr Phe Tyr Leu Lys Val Asn Gly Ser He Tyr Met Gly Met Trp Met 2610 2615 2620 Tyr Val Asp Val Cys Glu Cys Met Trp Met Tyr Val Asp Val Cys Gly 2625 2630 2635 2640 Cys Val Leu Trp He Cys He Cys Asp Tyr Val Trp He Tyr He Tyr 2645 2650 2655 He Tyr He Cys Leu Cys He Cys Val Phe Gly Tyr He Tyr Val Tyr 2660 2665 2670 Val Tyr Asp Phe Leu Tyr Met Tyr Leu Trp Val Lys Asp He Tyr He 2675 2680 2685 Trp Met Tyr Leu Tyr Val Phe Tyr He Tyr He Leu Tyr He Cys He 2690 2695 2700 Tyr He Lys Lys Glu He 2705 2710

Claims: WHAT IS CLAIMED IS: 1. A composition comprising an isolated DABP binding domain polypeptide. 2. The composition of claim -l , wherein the DABP binding domain polypeptide comprises between about 200 and about 300 amino acid residues. 3. The composition of claim 1, wherein the DABP binding domain polypeptide has residues 1 to about 325 of the amino acid sequence of SEQ ID No. 2. 4. The composition of claim 1, wherein the DABP binding region polypeptide is recombinantly produced. 5. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and an isolated DABP binding domain polypeptide in an amount sufficient to induce a protective immune response to Plasmodium vivax merozoites in an organism. 6. The composition of claim 5, further comprising an isolated SABP binding domain polypeptide in an amount sufficient to induce a protective immune response to Plasmodium falciparum merozoites in an organism. 7. A composition comprising an isolated SABP binding domain polypeptide. 8. The composition of claim 7, wherein the SABP binding domain polypeptide comprises between about 200 and about 600 amino acid residues. 9. The composition of claim 7, wherein the SABP binding domain polypeptide has residues 1 to about 616 of the amino acid sequence of SEQ ID No. 4. 10. The composition of claim 7, wherein the SABP binding region polypeptide is recombinantly produced. 11. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and an isolated SABP binding domain polypeptide in an amount sufficient to induce a protective immune response to Plasmodium falciparum merozoites in an organism. 12. The composition of claim 11, further comprising an isolated DABP binding domain polypeptide in an amount sufficient to induce a protective immune response to Plasmodium vivax merozoites in an organism. 13. A composition comprising an isolated polynucleotide which encodes a DABP binding domain polypeptide. 1 . The composition of claim 13 , wherein the polynucleotide encodes a DABP binding domain polypeptide having residues 1 to about 325 of the amino acid sequence of SEQ ID No. 2. 15. A recombinant cell comprising the polynucleotide of claim 13. 16. A composition comprising an isolated polynucleotide which encodes a SABP binding domain polypeptide. 17. The composition of claim 16, wherein the polynucleotide encodes a SABP binding domain polypeptide having residues 1 to about 616 of the amino acid sequence of SEQ ID No. 4. 18. A recombinant cell comprising the polynucleotide of claim 16. 19. A method of inducing a protective immune response to Plasmodium merozoites in a patient, the method comprising administration to the patient of an immunologically effective amount of a pharmaceutical composition comprising a pharmaceutically acceptable carrier and an isolated polypeptide selected from the group consisting of a DABP binding domain polypeptide, an SABP binding domain polypeptide and a combination thereof. 20. The method of claim 19, wherein the patient is a human. 21. A composition comprising a nucleotide sequence of the EBL gene family. 22. A composition comprising a nucleotide sequence of the ebl-el gene. 23. The composition of claim 22, wherein the ebl-el gene has the nucleotide sequence of SEQ ID No. 5. 24. A composition comprising the nucleotide sequence of the E31a gene. 25. The composition of claim 24, wherein the E31a gene has the nucleotide sequence of SEQ ID No. 7. 26. A composition comprising the nucleotide sequence of the Proj3 gene. 27. The composition of claim 26, wherein the Proj3 gene has the nucleotide sequence of SEQ ID No. 11. 28. A composition comprising the nucleotide sequence of the EBL-e2 gene. 29. The composition of claim 28, wherein the EBL-e2 gene has the nucleotide sequence of SEQ ID No. 9.

Inventors: CHITNIS CHETAN, MILLER LOUIS H, PETERSON DAVID S, SIM KIN LEE, SU XIN-ZHUAN, WELLEMS THOSMAS E, CHITNIS, CHETAN, MILLER, LOUIS, H., PETERSON, DAVID, S., SIM, KIN, LEE, SU, XIN-ZHUAN, WELLEMS, THOSMAS, E.
Applicants: US HEALTH, THE GOVERNMENT OF THE UNITED STATES OF AMERICA, RE
Application year: 1994
Main classification: C12N15
IPC codes: A61K39, A61P33, C07K14, C12N5, C12N15, C12P21, C12R1